[{"type":"journal_article","year":"2021","publisher":"Elsevier","doi":"10.1016/j.neuint.2021.104986","language":[{"iso":"eng"}],"date_published":"2021-05-01T00:00:00Z","_id":"9188","oa":1,"author":[{"id":"48EA0138-F248-11E8-B48F-1D18A9856A87","last_name":"Pauler","first_name":"Florian","full_name":"Pauler, Florian"},{"full_name":"Hudson, Quanah","first_name":"Quanah","last_name":"Hudson"},{"last_name":"Laukoter","id":"2D6B7A9A-F248-11E8-B48F-1D18A9856A87","full_name":"Laukoter, Susanne","first_name":"Susanne"},{"first_name":"Simon","full_name":"Hippenmeyer, Simon","orcid":"0000-0003-2279-1061","id":"37B36620-F248-11E8-B48F-1D18A9856A87","last_name":"Hippenmeyer"}],"intvolume":"       145","keyword":["Cell Biology","Cellular and Molecular Neuroscience"],"file_date_updated":"2021-08-11T12:30:38Z","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","ddc":["570"],"article_processing_charge":"Yes (via OA deal)","department":[{"_id":"SiHi"}],"acknowledgement":"We thank Melissa Stouffer for critically reading the manuscript. This work was supported by IST Austria institutional funds; NÖ Forschung und Bildung n[f + b] life science call grant (C13-002) to S.H. and the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation program (grant agreement 725780 LinPro) to S.H.","pmid":1,"article_number":"104986","date_created":"2021-02-23T12:31:43Z","article_type":"original","volume":145,"isi":1,"publication_identifier":{"issn":["0197-0186"]},"quality_controlled":"1","month":"05","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","status":"public","date_updated":"2023-08-07T13:48:26Z","abstract":[{"text":"Genomic imprinting is an epigenetic mechanism that results in parental allele-specific expression of ~1% of all genes in mouse and human. Imprinted genes are key developmental regulators and play pivotal roles in many biological processes such as nutrient transfer from the mother to offspring and neuronal development. Imprinted genes are also involved in human disease, including neurodevelopmental disorders, and often occur in clusters that are regulated by a common imprint control region (ICR). In extra-embryonic tissues ICRs can act over large distances, with the largest surrounding Igf2r spanning over 10 million base-pairs. Besides classical imprinted expression that shows near exclusive maternal or paternal expression, widespread biased imprinted expression has been identified mainly in brain. In this review we discuss recent developments mapping cell type specific imprinted expression in extra-embryonic tissues and neocortex in the mouse. We highlight the advantages of using an inducible uniparental chromosome disomy (UPD) system to generate cells carrying either two maternal or two paternal copies of a specific chromosome to analyze the functional consequences of genomic imprinting. Mosaic Analysis with Double Markers (MADM) allows fluorescent labeling and concomitant induction of UPD sparsely in specific cell types, and thus to over-express or suppress all imprinted genes on that chromosome. To illustrate the utility of this technique, we explain how MADM-induced UPD revealed new insights about the function of the well-studied Cdkn1c imprinted gene, and how MADM-induced UPDs led to identification of highly cell type specific phenotypes related to perturbed imprinted expression in the mouse neocortex. Finally, we give an outlook on how MADM could be used to probe cell type specific imprinted expression in other tissues in mouse, particularly in extra-embryonic tissues.","lang":"eng"}],"ec_funded":1,"tmp":{"image":"/images/cc_by_nc_nd.png","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"},"day":"01","oa_version":"Published Version","publication_status":"published","has_accepted_license":"1","scopus_import":"1","issue":"5","citation":{"ama":"Pauler F, Hudson Q, Laukoter S, Hippenmeyer S. Inducible uniparental chromosome disomy to probe genomic imprinting at single-cell level in brain and beyond. <i>Neurochemistry International</i>. 2021;145(5). doi:<a href=\"https://doi.org/10.1016/j.neuint.2021.104986\">10.1016/j.neuint.2021.104986</a>","mla":"Pauler, Florian, et al. “Inducible Uniparental Chromosome Disomy to Probe Genomic Imprinting at Single-Cell Level in Brain and Beyond.” <i>Neurochemistry International</i>, vol. 145, no. 5, 104986, Elsevier, 2021, doi:<a href=\"https://doi.org/10.1016/j.neuint.2021.104986\">10.1016/j.neuint.2021.104986</a>.","apa":"Pauler, F., Hudson, Q., Laukoter, S., &#38; Hippenmeyer, S. (2021). Inducible uniparental chromosome disomy to probe genomic imprinting at single-cell level in brain and beyond. <i>Neurochemistry International</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.neuint.2021.104986\">https://doi.org/10.1016/j.neuint.2021.104986</a>","ista":"Pauler F, Hudson Q, Laukoter S, Hippenmeyer S. 2021. Inducible uniparental chromosome disomy to probe genomic imprinting at single-cell level in brain and beyond. Neurochemistry International. 145(5), 104986.","short":"F. Pauler, Q. Hudson, S. Laukoter, S. Hippenmeyer, Neurochemistry International 145 (2021).","ieee":"F. Pauler, Q. Hudson, S. Laukoter, and S. Hippenmeyer, “Inducible uniparental chromosome disomy to probe genomic imprinting at single-cell level in brain and beyond,” <i>Neurochemistry International</i>, vol. 145, no. 5. Elsevier, 2021.","chicago":"Pauler, Florian, Quanah Hudson, Susanne Laukoter, and Simon Hippenmeyer. “Inducible Uniparental Chromosome Disomy to Probe Genomic Imprinting at Single-Cell Level in Brain and Beyond.” <i>Neurochemistry International</i>. Elsevier, 2021. <a href=\"https://doi.org/10.1016/j.neuint.2021.104986\">https://doi.org/10.1016/j.neuint.2021.104986</a>."},"project":[{"_id":"260018B0-B435-11E9-9278-68D0E5697425","name":"Principles of Neural Stem Cell Lineage Progression in Cerebral Cortex Development","call_identifier":"H2020","grant_number":"725780"},{"grant_number":"LS13-002","_id":"25D92700-B435-11E9-9278-68D0E5697425","name":"Mapping Cell-Type Specificity of the Genomic Imprintome in the Brain"}],"file":[{"success":1,"date_updated":"2021-08-11T12:30:38Z","file_id":"9883","checksum":"c6d7a40089cd29e289f9b22e75768304","date_created":"2021-08-11T12:30:38Z","file_size":7083499,"file_name":"2021_NCI_Pauler.pdf","content_type":"application/pdf","relation":"main_file","access_level":"open_access","creator":"kschuh"}],"title":"Inducible uniparental chromosome disomy to probe genomic imprinting at single-cell level in brain and beyond","external_id":{"pmid":["33600873"],"isi":["000635575000005"]},"publication":"Neurochemistry International"},{"citation":{"chicago":"Zeng, Longhui, Ivan Palaia, Anđela Šarić, and Xiaolei Su. “PLCγ1 Promotes Phase Separation of T Cell Signaling Components.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2021. <a href=\"https://doi.org/10.1083/jcb.202009154\">https://doi.org/10.1083/jcb.202009154</a>.","ieee":"L. Zeng, I. Palaia, A. Šarić, and X. Su, “PLCγ1 promotes phase separation of T cell signaling components,” <i>Journal of Cell Biology</i>, vol. 220, no. 6. Rockefeller University Press, 2021.","short":"L. Zeng, I. Palaia, A. Šarić, X. Su, Journal of Cell Biology 220 (2021).","mla":"Zeng, Longhui, et al. “PLCγ1 Promotes Phase Separation of T Cell Signaling Components.” <i>Journal of Cell Biology</i>, vol. 220, no. 6, e202009154, Rockefeller University Press, 2021, doi:<a href=\"https://doi.org/10.1083/jcb.202009154\">10.1083/jcb.202009154</a>.","ista":"Zeng L, Palaia I, Šarić A, Su X. 2021. PLCγ1 promotes phase separation of T cell signaling components. Journal of Cell Biology. 220(6), e202009154.","apa":"Zeng, L., Palaia, I., Šarić, A., &#38; Su, X. (2021). PLCγ1 promotes phase separation of T cell signaling components. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.202009154\">https://doi.org/10.1083/jcb.202009154</a>","ama":"Zeng L, Palaia I, Šarić A, Su X. PLCγ1 promotes phase separation of T cell signaling components. <i>Journal of Cell Biology</i>. 2021;220(6). doi:<a href=\"https://doi.org/10.1083/jcb.202009154\">10.1083/jcb.202009154</a>"},"issue":"6","scopus_import":"1","publication":"Journal of Cell Biology","external_id":{"pmid":["33929486"]},"title":"PLCγ1 promotes phase separation of T cell signaling components","date_updated":"2021-11-25T15:33:08Z","status":"public","license":"https://creativecommons.org/licenses/by-nc-sa/4.0/","oa_version":"None","publication_status":"published","tmp":{"image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)","short":"CC BY-NC-SA (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode"},"day":"30","abstract":[{"text":"The T cell receptor (TCR) pathway receives, processes, and amplifies the signal from pathogenic antigens to the activation of T cells. Although major components in this pathway have been identified, the knowledge on how individual components cooperate to effectively transduce signals remains limited. Phase separation emerges as a biophysical principle in organizing signaling molecules into liquid-like condensates. Here, we report that phospholipase Cγ1 (PLCγ1) promotes phase separation of LAT, a key adaptor protein in the TCR pathway. PLCγ1 directly cross-links LAT through its two SH2 domains. PLCγ1 also protects LAT from dephosphorylation by the phosphatase CD45 and promotes LAT-dependent ERK activation and SLP76 phosphorylation. Intriguingly, a nonmonotonic effect of PLCγ1 on LAT clustering was discovered. Computer simulations, based on patchy particles, revealed how the cluster size is regulated by protein compositions. Together, these results define a critical function of PLCγ1 in promoting phase separation of the LAT complex and TCR signal transduction.","lang":"eng"}],"date_created":"2021-11-25T15:21:30Z","article_number":"e202009154","pmid":1,"acknowledgement":"Charles H. Hood Foundation (NO AWARD) ; Rally Foundation (NO AWARD)","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","extern":"1","article_processing_charge":"No","keyword":["cell biology"],"intvolume":"       220","month":"04","quality_controlled":"1","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"article_type":"original","volume":220,"language":[{"iso":"eng"}],"doi":"10.1083/jcb.202009154","publisher":"Rockefeller University Press","year":"2021","type":"journal_article","author":[{"last_name":"Zeng","full_name":"Zeng, Longhui","first_name":"Longhui"},{"first_name":"Ivan","full_name":"Palaia, Ivan","last_name":"Palaia"},{"full_name":"Šarić, Anđela","first_name":"Anđela","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139"},{"full_name":"Su, Xiaolei","first_name":"Xiaolei","last_name":"Su"}],"_id":"10337","date_published":"2021-04-30T00:00:00Z"},{"author":[{"first_name":"Heike","full_name":"Rampelt, Heike","last_name":"Rampelt"},{"first_name":"Iva","full_name":"Sucec, Iva","last_name":"Sucec"},{"full_name":"Bersch, Beate","first_name":"Beate","last_name":"Bersch"},{"full_name":"Horten, Patrick","first_name":"Patrick","last_name":"Horten"},{"full_name":"Perschil, Inge","first_name":"Inge","last_name":"Perschil"},{"first_name":"Jean-Claude","full_name":"Martinou, Jean-Claude","last_name":"Martinou"},{"first_name":"Martin","full_name":"van der Laan, Martin","last_name":"van der Laan"},{"full_name":"Wiedemann, Nils","first_name":"Nils","last_name":"Wiedemann"},{"first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","orcid":"0000-0002-9350-7606"},{"first_name":"Nikolaus","full_name":"Pfanner, Nikolaus","last_name":"Pfanner"}],"oa":1,"_id":"8402","date_published":"2020-01-06T00:00:00Z","language":[{"iso":"eng"}],"doi":"10.1186/s12915-019-0733-6","publisher":"Springer Nature","year":"2020","type":"journal_article","month":"01","quality_controlled":"1","publication_identifier":{"issn":["1741-7007"]},"volume":18,"article_type":"original","article_number":"2","date_created":"2020-09-17T10:26:53Z","pmid":1,"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","keyword":["Biotechnology","Plant Science","General Biochemistry","Genetics and Molecular Biology","Developmental Biology","Cell Biology","Physiology","Ecology","Evolution","Behavior and Systematics","Structural Biology","General Agricultural and Biological Sciences"],"intvolume":"        18","publication_status":"published","oa_version":"Published Version","day":"06","abstract":[{"lang":"eng","text":"Background: The mitochondrial pyruvate carrier (MPC) plays a central role in energy metabolism by transporting pyruvate across the inner mitochondrial membrane. Its heterodimeric composition and homology to SWEET and semiSWEET transporters set the MPC apart from the canonical mitochondrial carrier family (named MCF or SLC25). The import of the canonical carriers is mediated by the carrier translocase of the inner membrane (TIM22) pathway and is dependent on their structure, which features an even number of transmembrane segments and both termini in the intermembrane space. The import pathway of MPC proteins has not been elucidated. The odd number of transmembrane segments and positioning of the N-terminus in the matrix argues against an import via the TIM22 carrier pathway but favors an import via the flexible presequence pathway.\r\nResults: Here, we systematically analyzed the import pathways of Mpc2 and Mpc3 and report that, contrary to an expected import via the flexible presequence pathway, yeast MPC proteins with an odd number of transmembrane segments and matrix-exposed N-terminus are imported by the carrier pathway, using the receptor Tom70, small TIM chaperones, and the TIM22 complex. The TIM9·10 complex chaperones MPC proteins through the mitochondrial intermembrane space using conserved hydrophobic motifs that are also required for the interaction with canonical carrier proteins.\r\nConclusions: The carrier pathway can import paired and non-paired transmembrane helices and translocate N-termini to either side of the mitochondrial inner membrane, revealing an unexpected versatility of the mitochondrial import pathway for non-cleavable inner membrane proteins."}],"date_updated":"2021-01-12T08:19:02Z","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1186/s12915-019-0733-6"}],"publication":"BMC Biology","external_id":{"pmid":["31907035"]},"title":"The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments","citation":{"apa":"Rampelt, H., Sucec, I., Bersch, B., Horten, P., Perschil, I., Martinou, J.-C., … Pfanner, N. (2020). The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. <i>BMC Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1186/s12915-019-0733-6\">https://doi.org/10.1186/s12915-019-0733-6</a>","mla":"Rampelt, Heike, et al. “The Mitochondrial Carrier Pathway Transports Non-Canonical Substrates with an Odd Number of Transmembrane Segments.” <i>BMC Biology</i>, vol. 18, 2, Springer Nature, 2020, doi:<a href=\"https://doi.org/10.1186/s12915-019-0733-6\">10.1186/s12915-019-0733-6</a>.","short":"H. Rampelt, I. Sucec, B. Bersch, P. Horten, I. Perschil, J.-C. Martinou, M. van der Laan, N. Wiedemann, P. Schanda, N. Pfanner, BMC Biology 18 (2020).","ista":"Rampelt H, Sucec I, Bersch B, Horten P, Perschil I, Martinou J-C, van der Laan M, Wiedemann N, Schanda P, Pfanner N. 2020. The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biology. 18, 2.","ama":"Rampelt H, Sucec I, Bersch B, et al. The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. <i>BMC Biology</i>. 2020;18. doi:<a href=\"https://doi.org/10.1186/s12915-019-0733-6\">10.1186/s12915-019-0733-6</a>","chicago":"Rampelt, Heike, Iva Sucec, Beate Bersch, Patrick Horten, Inge Perschil, Jean-Claude Martinou, Martin van der Laan, Nils Wiedemann, Paul Schanda, and Nikolaus Pfanner. “The Mitochondrial Carrier Pathway Transports Non-Canonical Substrates with an Odd Number of Transmembrane Segments.” <i>BMC Biology</i>. Springer Nature, 2020. <a href=\"https://doi.org/10.1186/s12915-019-0733-6\">https://doi.org/10.1186/s12915-019-0733-6</a>.","ieee":"H. Rampelt <i>et al.</i>, “The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments,” <i>BMC Biology</i>, vol. 18. Springer Nature, 2020."}},{"date_updated":"2023-09-05T15:41:48Z","status":"public","abstract":[{"text":"Efficient migration on adhesive surfaces involves the protrusion of lamellipodial actin networks and their subsequent stabilization by nascent adhesions. The actin-binding protein lamellipodin (Lpd) is thought to play a critical role in lamellipodium protrusion, by delivering Ena/VASP proteins onto the growing plus ends of actin filaments and by interacting with the WAVE regulatory complex, an activator of the Arp2/3 complex, at the leading edge. Using B16-F1 melanoma cell lines, we demonstrate that genetic ablation of Lpd compromises protrusion efficiency and coincident cell migration without altering essential parameters of lamellipodia, including their maximal rate of forward advancement and actin polymerization. We also confirmed lamellipodia and migration phenotypes with CRISPR/Cas9-mediated Lpd knockout Rat2 fibroblasts, excluding cell type-specific effects. Moreover, computer-aided analysis of cell-edge morphodynamics on B16-F1 cell lamellipodia revealed that loss of Lpd correlates with reduced temporal protrusion maintenance as a prerequisite of nascent adhesion formation. We conclude that Lpd optimizes protrusion and nascent adhesion formation by counteracting frequent, chaotic retraction and membrane ruffling.This article has an associated First Person interview with the first author of the paper. ","lang":"eng"}],"publication_status":"published","oa_version":"Published Version","day":"09","project":[{"grant_number":"M02495","call_identifier":"FWF","_id":"2674F658-B435-11E9-9278-68D0E5697425","name":"Protein structure and function in filopodia across scales"}],"citation":{"chicago":"Dimchev, Georgi A, Behnam Amiri, Ashley C. Humphries, Matthias Schaks, Vanessa Dimchev, Theresia E. B. Stradal, Jan Faix, et al. “Lamellipodin Tunes Cell Migration by Stabilizing Protrusions and Promoting Adhesion Formation.” <i>Journal of Cell Science</i>. The Company of Biologists, 2020. <a href=\"https://doi.org/10.1242/jcs.239020\">https://doi.org/10.1242/jcs.239020</a>.","ieee":"G. A. Dimchev <i>et al.</i>, “Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation,” <i>Journal of Cell Science</i>, vol. 133, no. 7. The Company of Biologists, 2020.","ista":"Dimchev GA, Amiri B, Humphries AC, Schaks M, Dimchev V, Stradal TEB, Faix J, Krause M, Way M, Falcke M, Rottner K. 2020. Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation. Journal of Cell Science. 133(7), jcs239020.","mla":"Dimchev, Georgi A., et al. “Lamellipodin Tunes Cell Migration by Stabilizing Protrusions and Promoting Adhesion Formation.” <i>Journal of Cell Science</i>, vol. 133, no. 7, jcs239020, The Company of Biologists, 2020, doi:<a href=\"https://doi.org/10.1242/jcs.239020\">10.1242/jcs.239020</a>.","apa":"Dimchev, G. A., Amiri, B., Humphries, A. C., Schaks, M., Dimchev, V., Stradal, T. E. B., … Rottner, K. (2020). Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation. <i>Journal of Cell Science</i>. The Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.239020\">https://doi.org/10.1242/jcs.239020</a>","short":"G.A. Dimchev, B. Amiri, A.C. Humphries, M. Schaks, V. Dimchev, T.E.B. Stradal, J. Faix, M. Krause, M. Way, M. Falcke, K. Rottner, Journal of Cell Science 133 (2020).","ama":"Dimchev GA, Amiri B, Humphries AC, et al. Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation. <i>Journal of Cell Science</i>. 2020;133(7). doi:<a href=\"https://doi.org/10.1242/jcs.239020\">10.1242/jcs.239020</a>"},"has_accepted_license":"1","issue":"7","external_id":{"isi":["000534387800005"],"pmid":[" 32094266"]},"title":"Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation","file":[{"file_id":"8435","date_created":"2020-09-17T14:07:51Z","checksum":"ba917e551acc4ece2884b751434df9ae","date_updated":"2020-10-11T22:30:02Z","file_name":"2020_JournalCellScience_Dimchev.pdf","file_size":13493302,"access_level":"open_access","relation":"main_file","content_type":"application/pdf","creator":"dernst","embargo":"2020-10-10"}],"publication":"Journal of Cell Science","publisher":"The Company of Biologists","year":"2020","language":[{"iso":"eng"}],"doi":"10.1242/jcs.239020","type":"journal_article","oa":1,"_id":"8434","author":[{"orcid":"0000-0001-8370-6161","id":"38C393BE-F248-11E8-B48F-1D18A9856A87","last_name":"Dimchev","first_name":"Georgi A","full_name":"Dimchev, Georgi A"},{"last_name":"Amiri","full_name":"Amiri, Behnam","first_name":"Behnam"},{"full_name":"Humphries, Ashley C.","first_name":"Ashley C.","last_name":"Humphries"},{"full_name":"Schaks, Matthias","first_name":"Matthias","last_name":"Schaks"},{"full_name":"Dimchev, Vanessa","first_name":"Vanessa","last_name":"Dimchev"},{"first_name":"Theresia E. B.","full_name":"Stradal, Theresia E. B.","last_name":"Stradal"},{"last_name":"Faix","first_name":"Jan","full_name":"Faix, Jan"},{"full_name":"Krause, Matthias","first_name":"Matthias","last_name":"Krause"},{"first_name":"Michael","full_name":"Way, Michael","last_name":"Way"},{"full_name":"Falcke, Martin","first_name":"Martin","last_name":"Falcke"},{"full_name":"Rottner, Klemens","first_name":"Klemens","last_name":"Rottner"}],"date_published":"2020-04-09T00:00:00Z","pmid":1,"acknowledgement":"This work was supported in part by Deutsche Forschungsgemeinschaft (DFG)[GRK2223/1, RO2414/5-1 (to K.R.), FA350/11-1 (to M.F.) and FA330/11-1 (to J.F.)],as well as by intramural funding from the Helmholtz Association (to T.E.B.S. andK.R.). G.D. was additionally funded by the Austrian Science Fund (FWF) LiseMeitner Program [M-2495]. A.C.H. and M.W. are supported by the Francis CrickInstitute, which receives its core funding from Cancer Research UK [FC001209], theMedical Research Council [FC001209] and the Wellcome Trust [FC001209]. M.K. issupported by the Biotechnology and Biological Sciences Research Council [BB/F011431/1, BB/J000590/1, BB/N000226/1]. Deposited in PMC for release after 6months.","department":[{"_id":"FlSc"}],"article_number":"jcs239020","date_created":"2020-09-17T14:00:33Z","keyword":["Cell Biology"],"intvolume":"       133","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","article_processing_charge":"No","ddc":["570"],"file_date_updated":"2020-10-11T22:30:02Z","quality_controlled":"1","publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"month":"04","article_type":"original","volume":133,"isi":1},{"status":"public","date_updated":"2022-07-18T08:31:52Z","day":"04","tmp":{"image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)","short":"CC BY-NC-SA (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode"},"publication_status":"published","oa_version":"Published Version","page":"433-444","abstract":[{"text":"Many adult tissues contain postmitotic cells as old as the host organism. The only organelle that does not turn over in these cells is the nucleus, and its maintenance represents a formidable challenge, as it harbors regulatory proteins that persist throughout adulthood. Here we developed strategies to visualize two classes of such long-lived proteins, histones and nucleoporins, to understand the function of protein longevity in nuclear maintenance. Genome-wide mapping of histones revealed specific enrichment of long-lived variants at silent gene loci. Interestingly, nuclear pores are maintained by piecemeal replacement of subunits, resulting in mosaic complexes composed of polypeptides with vastly different ages. In contrast, nondividing quiescent cells remove old nuclear pores in an ESCRT-dependent manner. Our findings reveal distinct molecular strategies of nuclear maintenance, linking lifelong protein persistence to gene regulation and nuclear integrity.","lang":"eng"}],"scopus_import":"1","issue":"2","has_accepted_license":"1","citation":{"mla":"Toyama, Brandon H., et al. “Visualization of Long-Lived Proteins Reveals Age Mosaicism within Nuclei of Postmitotic Cells.” <i>Journal of Cell Biology</i>, vol. 218, no. 2, Rockefeller University Press, 2019, pp. 433–44, doi:<a href=\"https://doi.org/10.1083/jcb.201809123\">10.1083/jcb.201809123</a>.","short":"B.H. Toyama, R. Arrojo e Drigo, V. Lev-Ram, R. Ramachandra, T.J. Deerinck, C. Lechene, M.H. Ellisman, M. Hetzer, Journal of Cell Biology 218 (2019) 433–444.","ista":"Toyama BH, Arrojo e Drigo R, Lev-Ram V, Ramachandra R, Deerinck TJ, Lechene C, Ellisman MH, Hetzer M. 2019. Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells. Journal of Cell Biology. 218(2), 433–444.","apa":"Toyama, B. H., Arrojo e Drigo, R., Lev-Ram, V., Ramachandra, R., Deerinck, T. J., Lechene, C., … Hetzer, M. (2019). Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201809123\">https://doi.org/10.1083/jcb.201809123</a>","ama":"Toyama BH, Arrojo e Drigo R, Lev-Ram V, et al. Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells. <i>Journal of Cell Biology</i>. 2019;218(2):433-444. doi:<a href=\"https://doi.org/10.1083/jcb.201809123\">10.1083/jcb.201809123</a>","chicago":"Toyama, Brandon H., Rafael Arrojo e Drigo, Varda Lev-Ram, Ranjan Ramachandra, Thomas J. Deerinck, Claude Lechene, Mark H. Ellisman, and Martin Hetzer. “Visualization of Long-Lived Proteins Reveals Age Mosaicism within Nuclei of Postmitotic Cells.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2019. <a href=\"https://doi.org/10.1083/jcb.201809123\">https://doi.org/10.1083/jcb.201809123</a>.","ieee":"B. H. Toyama <i>et al.</i>, “Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells,” <i>Journal of Cell Biology</i>, vol. 218, no. 2. Rockefeller University Press, pp. 433–444, 2019."},"publication":"Journal of Cell Biology","title":"Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells","file":[{"creator":"dernst","relation":"main_file","content_type":"application/pdf","access_level":"open_access","file_size":2503838,"file_name":"2019_JCB_Toyama.pdf","date_updated":"2022-04-08T08:26:32Z","success":1,"date_created":"2022-04-08T08:26:32Z","checksum":"7964ebbf833b0b35f9fba840eea9531d","file_id":"11139"}],"external_id":{"pmid":["30552100"]},"type":"journal_article","doi":"10.1083/jcb.201809123","language":[{"iso":"eng"}],"year":"2019","publisher":"Rockefeller University Press","date_published":"2019-02-04T00:00:00Z","author":[{"first_name":"Brandon H.","full_name":"Toyama, Brandon H.","last_name":"Toyama"},{"last_name":"Arrojo e Drigo","first_name":"Rafael","full_name":"Arrojo e Drigo, Rafael"},{"first_name":"Varda","full_name":"Lev-Ram, Varda","last_name":"Lev-Ram"},{"last_name":"Ramachandra","full_name":"Ramachandra, Ranjan","first_name":"Ranjan"},{"first_name":"Thomas J.","full_name":"Deerinck, Thomas J.","last_name":"Deerinck"},{"full_name":"Lechene, Claude","first_name":"Claude","last_name":"Lechene"},{"first_name":"Mark H.","full_name":"Ellisman, Mark H.","last_name":"Ellisman"},{"full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"_id":"11061","oa":1,"file_date_updated":"2022-04-08T08:26:32Z","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","ddc":["570"],"extern":"1","intvolume":"       218","keyword":["Cell Biology"],"date_created":"2022-04-07T07:45:11Z","pmid":1,"article_type":"original","volume":218,"month":"02","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"quality_controlled":"1"},{"citation":{"ieee":"R. Arrojo e Drigo <i>et al.</i>, “Age mosaicism across multiple scales in adult tissues,” <i>Cell Metabolism</i>, vol. 30, no. 2. Elsevier, p. 343–351.e3, 2019.","chicago":"Arrojo e Drigo, Rafael, Varda Lev-Ram, Swati Tyagi, Ranjan Ramachandra, Thomas Deerinck, Eric Bushong, Sebastien Phan, et al. “Age Mosaicism across Multiple Scales in Adult Tissues.” <i>Cell Metabolism</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">https://doi.org/10.1016/j.cmet.2019.05.010</a>.","ama":"Arrojo e Drigo R, Lev-Ram V, Tyagi S, et al. Age mosaicism across multiple scales in adult tissues. <i>Cell Metabolism</i>. 2019;30(2):343-351.e3. doi:<a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">10.1016/j.cmet.2019.05.010</a>","short":"R. Arrojo e Drigo, V. Lev-Ram, S. Tyagi, R. Ramachandra, T. Deerinck, E. Bushong, S. Phan, V. Orphan, C. Lechene, M.H. Ellisman, M. Hetzer, Cell Metabolism 30 (2019) 343–351.e3.","apa":"Arrojo e Drigo, R., Lev-Ram, V., Tyagi, S., Ramachandra, R., Deerinck, T., Bushong, E., … Hetzer, M. (2019). Age mosaicism across multiple scales in adult tissues. <i>Cell Metabolism</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">https://doi.org/10.1016/j.cmet.2019.05.010</a>","ista":"Arrojo e Drigo R, Lev-Ram V, Tyagi S, Ramachandra R, Deerinck T, Bushong E, Phan S, Orphan V, Lechene C, Ellisman MH, Hetzer M. 2019. Age mosaicism across multiple scales in adult tissues. Cell Metabolism. 30(2), 343–351.e3.","mla":"Arrojo e Drigo, Rafael, et al. “Age Mosaicism across Multiple Scales in Adult Tissues.” <i>Cell Metabolism</i>, vol. 30, no. 2, Elsevier, 2019, p. 343–351.e3, doi:<a href=\"https://doi.org/10.1016/j.cmet.2019.05.010\">10.1016/j.cmet.2019.05.010</a>."},"issue":"2","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1016/j.cmet.2019.05.010","open_access":"1"}],"external_id":{"pmid":["31178361"]},"title":"Age mosaicism across multiple scales in adult tissues","publication":"Cell Metabolism","date_updated":"2022-07-18T08:32:30Z","status":"public","abstract":[{"text":"Most neurons are not replaced during an animal’s lifetime. This nondividing state is characterized by extreme longevity and age-dependent decline of key regulatory proteins. To study the lifespans of cells and proteins in adult tissues, we combined isotope labeling of mice with a hybrid imaging method (MIMS-EM). Using 15N mapping, we show that liver and pancreas are composed of cells with vastly different ages, many as old as the animal. Strikingly, we also found that a subset of fibroblasts and endothelial cells, both known for their replicative potential, are characterized by the absence of cell division during adulthood. In addition, we show that the primary cilia of beta cells and neurons contains different structural regions with vastly different lifespans. Based on these results, we propose that age mosaicism across multiple scales is a fundamental principle of adult tissue, cell, and protein complex organization.","lang":"eng"}],"publication_status":"published","page":"343-351.e3","oa_version":"Published Version","day":"06","pmid":1,"date_created":"2022-04-07T07:45:21Z","keyword":["Cell Biology","Molecular Biology","Physiology"],"intvolume":"        30","article_processing_charge":"No","extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","quality_controlled":"1","publication_identifier":{"issn":["1550-4131"]},"month":"08","volume":30,"article_type":"original","publisher":"Elsevier","year":"2019","language":[{"iso":"eng"}],"doi":"10.1016/j.cmet.2019.05.010","type":"journal_article","oa":1,"_id":"11062","author":[{"full_name":"Arrojo e Drigo, Rafael","first_name":"Rafael","last_name":"Arrojo e Drigo"},{"last_name":"Lev-Ram","first_name":"Varda","full_name":"Lev-Ram, Varda"},{"first_name":"Swati","full_name":"Tyagi, Swati","last_name":"Tyagi"},{"first_name":"Ranjan","full_name":"Ramachandra, Ranjan","last_name":"Ramachandra"},{"full_name":"Deerinck, Thomas","first_name":"Thomas","last_name":"Deerinck"},{"last_name":"Bushong","first_name":"Eric","full_name":"Bushong, Eric"},{"first_name":"Sebastien","full_name":"Phan, Sebastien","last_name":"Phan"},{"full_name":"Orphan, Victoria","first_name":"Victoria","last_name":"Orphan"},{"first_name":"Claude","full_name":"Lechene, Claude","last_name":"Lechene"},{"first_name":"Mark H.","full_name":"Ellisman, Mark H.","last_name":"Ellisman"},{"full_name":"HETZER, Martin W","first_name":"Martin W","orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER"}],"date_published":"2019-08-06T00:00:00Z"},{"type":"dissertation","publisher":"Institute of Science and Technology Austria","year":"2019","language":[{"iso":"eng"}],"doi":"10.15479/AT:ISTA:6891","date_published":"2019-07-24T00:00:00Z","oa":1,"_id":"6891","author":[{"first_name":"Aglaja","full_name":"Kopf, Aglaja","orcid":"0000-0002-2187-6656","last_name":"Kopf","id":"31DAC7B6-F248-11E8-B48F-1D18A9856A87"}],"keyword":["cell biology","immunology","leukocyte","migration","microfluidics"],"article_processing_charge":"No","ddc":["570"],"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","file_date_updated":"2020-10-17T22:30:03Z","department":[{"_id":"MiSi"}],"date_created":"2019-09-19T08:19:44Z","supervisor":[{"last_name":"Sixt","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179","first_name":"Michael K","full_name":"Sixt, Michael K"}],"publication_identifier":{"eissn":["2663-337X"],"isbn":["978-3-99078-002-2"]},"month":"07","status":"public","date_updated":"2023-10-18T08:49:17Z","abstract":[{"text":"While cells of mesenchymal or epithelial origin perform their effector functions in a purely anchorage dependent manner, cells derived from the hematopoietic lineage are not committed to operate only within a specific niche. Instead, these cells are able to function autonomously of the molecular composition in a broad range of tissue compartments. By this means, cells of the hematopoietic lineage retain the capacity to disseminate into connective tissue and recirculate between organs, building the foundation for essential processes such as tissue regeneration or immune surveillance. \r\nCells of the immune system, specifically leukocytes, are extraordinarily good at performing this task. These cells are able to flexibly shift their mode of migration between an adhesion-mediated and an adhesion-independent manner, instantaneously accommodating for any changes in molecular composition of the external scaffold. The key component driving directed leukocyte migration is the chemokine receptor 7, which guides the cell along gradients of chemokine ligand. Therefore, the physical destination of migrating leukocytes is purely deterministic, i.e. given by global directional cues such as chemokine gradients. \r\nNevertheless, these cells typically reside in three-dimensional scaffolds of inhomogeneous complexity, raising the question whether cells are able to locally discriminate between multiple optional migration routes. Current literature provides evidence that leukocytes, specifically dendritic cells, do indeed probe their surrounding by virtue of multiple explorative protrusions. However, it remains enigmatic how these cells decide which one is the more favorable route to follow and what are the key players involved in performing this task. Due to the heterogeneous environment of most tissues, and the vast adaptability of migrating leukocytes, at this time it is not clear to what extent leukocytes are able to optimize their migratory strategy by adapting their level of adhesiveness. And, given the fact that leukocyte migration is characterized by branched cell shapes in combination with high migration velocities, it is reasonable to assume that these cells require fine tuned shape maintenance mechanisms that tightly coordinate protrusion and adhesion dynamics in a spatiotemporal manner. \r\nTherefore, this study aimed to elucidate how rapidly migrating leukocytes opt for an ideal migratory path while maintaining a continuous cell shape and balancing adhesive forces to efficiently navigate through complex microenvironments. \r\nThe results of this study unraveled a role for the microtubule cytoskeleton in promoting the decision making process during path finding and for the first time point towards a microtubule-mediated function in cell shape maintenance of highly ramified cells such as dendritic cells. Furthermore, we found that migrating low-adhesive leukocytes are able to instantaneously adapt to increased tensile load by engaging adhesion receptors. This response was only occurring tangential to the substrate while adhesive properties in the vertical direction were not increased. As leukocytes are primed for rapid migration velocities, these results demonstrate that leukocyte integrins are able to confer a high level of traction forces parallel to the cell membrane along the direction of migration without wasting energy in gluing the cell to the substrate. \r\nThus, the data in the here presented thesis provide new insights into the pivotal role of cytoskeletal dynamics and the mechanisms of force transduction during leukocyte migration. \r\nThereby the here presented results help to further define fundamental principles underlying leukocyte migration and open up potential therapeutic avenues of clinical relevance.\r\n","lang":"eng"}],"page":"171","oa_version":"Published Version","publication_status":"published","day":"24","degree_awarded":"PhD","alternative_title":["ISTA Thesis"],"has_accepted_license":"1","project":[{"name":"Nano-Analytics of Cellular Systems","_id":"265E2996-B435-11E9-9278-68D0E5697425","grant_number":"W01250-B20","call_identifier":"FWF"}],"citation":{"chicago":"Kopf, Aglaja. “The Implication of Cytoskeletal Dynamics on Leukocyte Migration.” Institute of Science and Technology Austria, 2019. <a href=\"https://doi.org/10.15479/AT:ISTA:6891\">https://doi.org/10.15479/AT:ISTA:6891</a>.","ieee":"A. Kopf, “The implication of cytoskeletal dynamics on leukocyte migration,” Institute of Science and Technology Austria, 2019.","short":"A. Kopf, The Implication of Cytoskeletal Dynamics on Leukocyte Migration, Institute of Science and Technology Austria, 2019.","apa":"Kopf, A. (2019). <i>The implication of cytoskeletal dynamics on leukocyte migration</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:6891\">https://doi.org/10.15479/AT:ISTA:6891</a>","mla":"Kopf, Aglaja. <i>The Implication of Cytoskeletal Dynamics on Leukocyte Migration</i>. Institute of Science and Technology Austria, 2019, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:6891\">10.15479/AT:ISTA:6891</a>.","ista":"Kopf A. 2019. The implication of cytoskeletal dynamics on leukocyte migration. Institute of Science and Technology Austria.","ama":"Kopf A. The implication of cytoskeletal dynamics on leukocyte migration. 2019. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:6891\">10.15479/AT:ISTA:6891</a>"},"related_material":{"link":[{"relation":"press_release","url":"https://ist.ac.at/en/news/feeling-like-a-cell/"}],"record":[{"id":"6328","status":"public","relation":"part_of_dissertation"},{"relation":"part_of_dissertation","id":"15","status":"public"},{"status":"public","id":"6877","relation":"part_of_dissertation"}]},"file":[{"creator":"akopf","access_level":"closed","relation":"source_file","content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","file_name":"Kopf_PhD_Thesis.docx","file_size":74735267,"checksum":"00d100d6468e31e583051e0a006b640c","date_created":"2019-10-15T05:28:42Z","file_id":"6950","embargo_to":"open_access","date_updated":"2020-10-17T22:30:03Z"},{"content_type":"application/pdf","relation":"main_file","access_level":"open_access","embargo":"2020-10-16","creator":"akopf","date_updated":"2020-10-17T22:30:03Z","checksum":"5d1baa899993ae6ca81aebebe1797000","date_created":"2019-10-15T05:28:47Z","file_id":"6951","file_size":52787224,"file_name":"Kopf_PhD_Thesis1.pdf"}],"title":"The implication of cytoskeletal dynamics on leukocyte migration"},{"abstract":[{"text":"Background\r\nESCRT-III is a membrane remodelling filament with the unique ability to cut membranes from the inside of the membrane neck. It is essential for the final stage of cell division, the formation of vesicles, the release of viruses, and membrane repair. Distinct from other cytoskeletal filaments, ESCRT-III filaments do not consume energy themselves, but work in conjunction with another ATP-consuming complex. Despite rapid progress in describing the cell biology of ESCRT-III, we lack an understanding of the physical mechanisms behind its force production and membrane remodelling.\r\nResults\r\nHere we present a minimal coarse-grained model that captures all the experimentally reported cases of ESCRT-III driven membrane sculpting, including the formation of downward and upward cones and tubules. This model suggests that a change in the geometry of membrane bound ESCRT-III filaments—from a flat spiral to a 3D helix—drives membrane deformation. We then show that such repetitive filament geometry transitions can induce the fission of cargo-containing vesicles.\r\nConclusions\r\nOur model provides a general physical mechanism that explains the full range of ESCRT-III-dependent membrane remodelling and scission events observed in cells. This mechanism for filament force production is distinct from the mechanisms described for other cytoskeletal elements discovered so far. The mechanistic principles revealed here suggest new ways of manipulating ESCRT-III-driven processes in cells and could be used to guide the engineering of synthetic membrane-sculpting systems.","lang":"eng"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"day":"22","oa_version":"Published Version","publication_status":"published","license":"https://creativecommons.org/licenses/by/4.0/","status":"public","date_updated":"2021-11-26T11:54:29Z","title":"Changes in ESCRT-III filament geometry drive membrane remodelling and fission in silico","file":[{"file_size":1648926,"file_name":"2019_BMCBio_Harker_Kirschneck.pdf","date_updated":"2021-11-26T11:37:54Z","success":1,"date_created":"2021-11-26T11:37:54Z","checksum":"31d8bae55a376d30925f53f7e1a02396","file_id":"10356","creator":"cchlebak","relation":"main_file","content_type":"application/pdf","access_level":"open_access"}],"external_id":{"pmid":["31640700"]},"publication":"BMC Biology","main_file_link":[{"open_access":"1","url":"https://www.biorxiv.org/content/10.1101/559898"}],"has_accepted_license":"1","scopus_import":"1","issue":"1","citation":{"chicago":"Harker-Kirschneck, Lena, Buzz Baum, and Anđela Šarić. “Changes in ESCRT-III Filament Geometry Drive Membrane Remodelling and Fission in Silico.” <i>BMC Biology</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1186/s12915-019-0700-2\">https://doi.org/10.1186/s12915-019-0700-2</a>.","ieee":"L. Harker-Kirschneck, B. Baum, and A. Šarić, “Changes in ESCRT-III filament geometry drive membrane remodelling and fission in silico,” <i>BMC Biology</i>, vol. 17, no. 1. Springer Nature, 2019.","apa":"Harker-Kirschneck, L., Baum, B., &#38; Šarić, A. (2019). Changes in ESCRT-III filament geometry drive membrane remodelling and fission in silico. <i>BMC Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1186/s12915-019-0700-2\">https://doi.org/10.1186/s12915-019-0700-2</a>","short":"L. Harker-Kirschneck, B. Baum, A. Šarić, BMC Biology 17 (2019).","ista":"Harker-Kirschneck L, Baum B, Šarić A. 2019. Changes in ESCRT-III filament geometry drive membrane remodelling and fission in silico. BMC Biology. 17(1), 82.","mla":"Harker-Kirschneck, Lena, et al. “Changes in ESCRT-III Filament Geometry Drive Membrane Remodelling and Fission in Silico.” <i>BMC Biology</i>, vol. 17, no. 1, 82, Springer Nature, 2019, doi:<a href=\"https://doi.org/10.1186/s12915-019-0700-2\">10.1186/s12915-019-0700-2</a>.","ama":"Harker-Kirschneck L, Baum B, Šarić A. Changes in ESCRT-III filament geometry drive membrane remodelling and fission in silico. <i>BMC Biology</i>. 2019;17(1). doi:<a href=\"https://doi.org/10.1186/s12915-019-0700-2\">10.1186/s12915-019-0700-2</a>"},"date_published":"2019-10-22T00:00:00Z","_id":"10354","oa":1,"author":[{"last_name":"Harker-Kirschneck","first_name":"Lena","full_name":"Harker-Kirschneck, Lena"},{"last_name":"Baum","full_name":"Baum, Buzz","first_name":"Buzz"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","orcid":"0000-0002-7854-2139","first_name":"Anđela","full_name":"Šarić, Anđela"}],"type":"journal_article","year":"2019","publisher":"Springer Nature","doi":"10.1186/s12915-019-0700-2","language":[{"iso":"eng"}],"volume":17,"article_type":"original","publication_identifier":{"issn":["1741-7007"]},"quality_controlled":"1","month":"10","intvolume":"        17","keyword":["cell biology"],"file_date_updated":"2021-11-26T11:37:54Z","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","ddc":["570"],"extern":"1","acknowledgement":"We thank Jeremy Carlton, Mike Staddon, Geraint Harker, and the Wellcome Trust Consortium “Archaeal Origins of Eukaryotic Cell Organisation” for fruitful conversations. We thank Peter Wirnsberger and Tine Curk for discussions about the membrane model implementation.","pmid":1,"article_number":"82","date_created":"2021-11-26T11:25:03Z"},{"status":"public","type":"journal_article","doi":"10.1074/jbc.ra118.002251","language":[{"iso":"eng"}],"year":"2018","date_updated":"2021-01-12T08:19:17Z","publisher":"American Society for Biochemistry & Molecular Biology","day":"01","page":"8379-8393","oa_version":"None","publication_status":"published","date_published":"2018-06-01T00:00:00Z","abstract":[{"lang":"eng","text":"Mycobacterium tuberculosis can remain dormant in the host, an ability that explains the failure of many current tuberculosis treatments. Recently, the natural products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein substrates, such as proteins containing phosphorylated arginine residues, to the ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain. Cyclomarin binding to this domain specifically blocked these N-terminal dynamics. On the basis of these results, we propose a mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics, which modulates the chaperone enzymatic activity leading eventually to cell death."}],"author":[{"full_name":"Weinhäupl, Katharina","first_name":"Katharina","last_name":"Weinhäupl"},{"last_name":"Brennich","full_name":"Brennich, Martha","first_name":"Martha"},{"first_name":"Uli","full_name":"Kazmaier, Uli","last_name":"Kazmaier"},{"last_name":"Lelievre","first_name":"Joel","full_name":"Lelievre, Joel"},{"last_name":"Ballell","full_name":"Ballell, Lluis","first_name":"Lluis"},{"full_name":"Goldberg, Alfred","first_name":"Alfred","last_name":"Goldberg"},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul"},{"full_name":"Fraga, Hugo","first_name":"Hugo","last_name":"Fraga"}],"_id":"8440","issue":"22","extern":"1","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":"       293","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"date_created":"2020-09-18T10:05:18Z","citation":{"short":"K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg, P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.","apa":"Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg, A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>","mla":"Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22, American Society for Biochemistry &#38; Molecular Biology, 2018, pp. 8379–93, doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>.","ista":"Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 293(22), 8379–8393.","ama":"Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. 2018;293(22):8379-8393. doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>","chicago":"Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology, 2018. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>.","ieee":"K. Weinhäupl <i>et al.</i>, “The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22. American Society for Biochemistry &#38; Molecular Biology, pp. 8379–8393, 2018."},"publication":"Journal of Biological Chemistry","title":"The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis","article_type":"original","volume":293,"month":"06","publication_identifier":{"issn":["0021-9258","1083-351X"]},"quality_controlled":"1"},{"issue":"5","scopus_import":"1","citation":{"ista":"Toda T, Hsu JY, Linker SB, Hu L, Schafer ST, Mertens J, Jacinto FV, Hetzer M, Gage FH. 2017. Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. Cell Stem Cell. 21(5), 618–634.e7.","apa":"Toda, T., Hsu, J. Y., Linker, S. B., Hu, L., Schafer, S. T., Mertens, J., … Gage, F. H. (2017). Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. <i>Cell Stem Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">https://doi.org/10.1016/j.stem.2017.08.012</a>","short":"T. Toda, J.Y. Hsu, S.B. Linker, L. Hu, S.T. Schafer, J. Mertens, F.V. Jacinto, M. Hetzer, F.H. Gage, Cell Stem Cell 21 (2017) 618–634.e7.","mla":"Toda, Tomohisa, et al. “Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells.” <i>Cell Stem Cell</i>, vol. 21, no. 5, Elsevier, 2017, p. 618–634.e7, doi:<a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">10.1016/j.stem.2017.08.012</a>.","ama":"Toda T, Hsu JY, Linker SB, et al. Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells. <i>Cell Stem Cell</i>. 2017;21(5):618-634.e7. doi:<a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">10.1016/j.stem.2017.08.012</a>","chicago":"Toda, Tomohisa, Jonathan Y. Hsu, Sara B. Linker, Lauren Hu, Simon T. Schafer, Jerome Mertens, Filipe V. Jacinto, Martin Hetzer, and Fred H. Gage. “Nup153 Interacts with Sox2 to Enable Bimodal Gene Regulation and Maintenance of Neural Progenitor Cells.” <i>Cell Stem Cell</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.stem.2017.08.012\">https://doi.org/10.1016/j.stem.2017.08.012</a>.","ieee":"T. Toda <i>et al.</i>, “Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells,” <i>Cell Stem Cell</i>, vol. 21, no. 5. Elsevier, p. 618–634.e7, 2017."},"external_id":{"pmid":["28919367"]},"title":"Nup153 interacts with Sox2 to enable bimodal gene regulation and maintenance of neural progenitor cells","publication":"Cell Stem Cell","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.stem.2017.08.012"}],"status":"public","date_updated":"2022-07-18T08:33:07Z","abstract":[{"lang":"eng","text":"Neural progenitor cells (NeuPCs) possess a unique nuclear architecture that changes during differentiation. Nucleoporins are linked with cell-type-specific gene regulation, coupling physical changes in nuclear structure to transcriptional output; but, whether and how they coordinate with key fate-determining transcription factors is unclear. Here we show that the nucleoporin Nup153 interacts with Sox2 in adult NeuPCs, where it is indispensable for their maintenance and controls neuronal differentiation. Genome-wide analyses show that Nup153 and Sox2 bind and co-regulate hundreds of genes. Binding of Nup153 to gene promoters or transcriptional end sites correlates with increased or decreased gene expression, respectively, and inhibiting Nup153 expression alters open chromatin configurations at its target genes, disrupts genomic localization of Sox2, and promotes differentiation in vitro and a gliogenic fate switch in vivo. Together, these findings reveal that nuclear structural proteins may exert bimodal transcriptional effects to control cell fate."}],"publication_status":"published","oa_version":"Published Version","page":"618-634.e7","day":"02","keyword":["Cell Biology","Genetics","Molecular Medicine"],"intvolume":"        21","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","article_processing_charge":"No","pmid":1,"date_created":"2022-04-07T07:46:12Z","article_type":"original","volume":21,"quality_controlled":"1","publication_identifier":{"issn":["1934-5909"]},"month":"11","type":"journal_article","publisher":"Elsevier","year":"2017","language":[{"iso":"eng"}],"doi":"10.1016/j.stem.2017.08.012","date_published":"2017-11-02T00:00:00Z","oa":1,"_id":"11067","author":[{"last_name":"Toda","first_name":"Tomohisa","full_name":"Toda, Tomohisa"},{"last_name":"Hsu","full_name":"Hsu, Jonathan Y.","first_name":"Jonathan Y."},{"last_name":"Linker","full_name":"Linker, Sara B.","first_name":"Sara B."},{"last_name":"Hu","full_name":"Hu, Lauren","first_name":"Lauren"},{"last_name":"Schafer","first_name":"Simon T.","full_name":"Schafer, Simon T."},{"last_name":"Mertens","full_name":"Mertens, Jerome","first_name":"Jerome"},{"first_name":"Filipe V.","full_name":"Jacinto, Filipe V.","last_name":"Jacinto"},{"first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X"},{"full_name":"Gage, Fred H.","first_name":"Fred H.","last_name":"Gage"}]},{"date_updated":"2022-07-18T08:33:47Z","status":"public","abstract":[{"text":"Repeated rounds of nuclear envelope (NE) rupture and repair have been observed in laminopathy and cancer cells and result in intermittent loss of nucleus compartmentalization. Currently, the causes of NE rupture are unclear. Here, we show that NE rupture in cancer cells relies on the assembly of contractile actin bundles that interact with the nucleus via the linker of nucleoskeleton and cytoskeleton (LINC) complex. We found that the loss of actin bundles or the LINC complex did not rescue nuclear lamina defects, a previously identified determinant of nuclear membrane stability, but did decrease the number and size of chromatin hernias. Finally, NE rupture inhibition could be rescued in cells treated with actin-depolymerizing drugs by mechanically constraining nucleus height. These data suggest a model of NE rupture where weak membrane areas, caused by defects in lamina organization, rupture because of an increase in intranuclear pressure from actin-based nucleus confinement.","lang":"eng"}],"publication_status":"published","oa_version":"Published Version","page":"27-36","day":"03","citation":{"ieee":"E. M. Hatch and M. Hetzer, “Nuclear envelope rupture is induced by actin-based nucleus confinement,” <i>Journal of Cell Biology</i>, vol. 215, no. 1. Rockefeller University Press, pp. 27–36, 2016.","chicago":"Hatch, Emily M., and Martin Hetzer. “Nuclear Envelope Rupture Is Induced by Actin-Based Nucleus Confinement.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2016. <a href=\"https://doi.org/10.1083/jcb.201603053\">https://doi.org/10.1083/jcb.201603053</a>.","ama":"Hatch EM, Hetzer M. Nuclear envelope rupture is induced by actin-based nucleus confinement. <i>Journal of Cell Biology</i>. 2016;215(1):27-36. doi:<a href=\"https://doi.org/10.1083/jcb.201603053\">10.1083/jcb.201603053</a>","mla":"Hatch, Emily M., and Martin Hetzer. “Nuclear Envelope Rupture Is Induced by Actin-Based Nucleus Confinement.” <i>Journal of Cell Biology</i>, vol. 215, no. 1, Rockefeller University Press, 2016, pp. 27–36, doi:<a href=\"https://doi.org/10.1083/jcb.201603053\">10.1083/jcb.201603053</a>.","short":"E.M. Hatch, M. Hetzer, Journal of Cell Biology 215 (2016) 27–36.","apa":"Hatch, E. M., &#38; Hetzer, M. (2016). Nuclear envelope rupture is induced by actin-based nucleus confinement. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201603053\">https://doi.org/10.1083/jcb.201603053</a>","ista":"Hatch EM, Hetzer M. 2016. Nuclear envelope rupture is induced by actin-based nucleus confinement. Journal of Cell Biology. 215(1), 27–36."},"issue":"1","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1083/jcb.201603053","open_access":"1"}],"external_id":{"pmid":["27697922"]},"title":"Nuclear envelope rupture is induced by actin-based nucleus confinement","publication":"Journal of Cell Biology","publisher":"Rockefeller University Press","year":"2016","language":[{"iso":"eng"}],"doi":"10.1083/jcb.201603053","type":"journal_article","oa":1,"_id":"11069","author":[{"last_name":"Hatch","first_name":"Emily M.","full_name":"Hatch, Emily M."},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W"}],"date_published":"2016-10-03T00:00:00Z","pmid":1,"date_created":"2022-04-07T07:47:42Z","keyword":["Cell Biology"],"intvolume":"       215","article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","quality_controlled":"1","publication_identifier":{"issn":["0021-9525","1540-8140"]},"month":"10","article_type":"original","volume":215},{"_id":"11075","author":[{"last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J. Sebastian","first_name":"J. Sebastian"},{"first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X"}],"date_published":"2015-03-16T00:00:00Z","year":"2015","publisher":"Rockefeller University Press","doi":"10.1083/jcb.201410047","language":[{"iso":"eng"}],"type":"journal_article","publication_identifier":{"issn":["0021-9525"],"eissn":["1540-8140"]},"quality_controlled":"1","month":"03","volume":208,"article_type":"original","pmid":1,"date_created":"2022-04-07T07:49:10Z","intvolume":"       208","keyword":["Cell Biology"],"article_processing_charge":"No","extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","abstract":[{"lang":"eng","text":"Previously, we identified the nucleoporin gp210/Nup210 as a critical regulator of muscle and neuronal differentiation, but how this nucleoporin exerts its function and whether it modulates nuclear pore complex (NPC) activity remain unknown. Here, we show that gp210/Nup210 mediates muscle cell differentiation in vitro via its conserved N-terminal domain that extends into the perinuclear space. Removal of the C-terminal domain, which partially mislocalizes gp210/Nup210 away from NPCs, efficiently rescues the differentiation defect caused by the knockdown of endogenous gp210/Nup210. Unexpectedly, a gp210/Nup210 mutant lacking the NPC-targeting transmembrane and C-terminal domains is sufficient for C2C12 myoblast differentiation. We demonstrate that the endoplasmic reticulum (ER) stress-specific caspase cascade is exacerbated during Nup210 depletion and that blocking ER stress-mediated apoptosis rescues differentiation of Nup210-deficient cells. Our results suggest that the role of gp210/Nup210 in cell differentiation is mediated by its large luminal domain, which can act independently of NPC association and appears to play a pivotal role in the maintenance of nuclear envelope/ER homeostasis."}],"day":"16","page":"671-681","oa_version":"Published Version","publication_status":"published","date_updated":"2022-07-18T08:43:00Z","status":"public","title":"The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis","external_id":{"pmid":["25778917"]},"publication":"Journal of Cell Biology","citation":{"chicago":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210 Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2015. <a href=\"https://doi.org/10.1083/jcb.201410047\">https://doi.org/10.1083/jcb.201410047</a>.","ieee":"J. S. Gomez-Cavazos and M. Hetzer, “The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis,” <i>Journal of Cell Biology</i>, vol. 208, no. 6. Rockefeller University Press, pp. 671–681, 2015.","ista":"Gomez-Cavazos JS, Hetzer M. 2015. The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. Journal of Cell Biology. 208(6), 671–681.","short":"J.S. Gomez-Cavazos, M. Hetzer, Journal of Cell Biology 208 (2015) 671–681.","apa":"Gomez-Cavazos, J. S., &#38; Hetzer, M. (2015). The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201410047\">https://doi.org/10.1083/jcb.201410047</a>","mla":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210 Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.” <i>Journal of Cell Biology</i>, vol. 208, no. 6, Rockefeller University Press, 2015, pp. 671–81, doi:<a href=\"https://doi.org/10.1083/jcb.201410047\">10.1083/jcb.201410047</a>.","ama":"Gomez-Cavazos JS, Hetzer M. The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. <i>Journal of Cell Biology</i>. 2015;208(6):671-681. doi:<a href=\"https://doi.org/10.1083/jcb.201410047\">10.1083/jcb.201410047</a>"},"scopus_import":"1","issue":"6"},{"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.cels.2015.08.012"}],"publication":"Cell Systems","title":"Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats","external_id":{"pmid":["27135913"]},"citation":{"ista":"Ori A, Toyama BH, Harris MS, Bock T, Iskar M, Bork P, Ingolia NT, Hetzer M, Beck M. 2015. Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats. Cell Systems. 1(3), P224-237.","apa":"Ori, A., Toyama, B. H., Harris, M. S., Bock, T., Iskar, M., Bork, P., … Beck, M. (2015). Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats. <i>Cell Systems</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cels.2015.08.012\">https://doi.org/10.1016/j.cels.2015.08.012</a>","mla":"Ori, Alessandro, et al. “Integrated Transcriptome and Proteome Analyses Reveal Organ-Specific Proteome Deterioration in Old Rats.” <i>Cell Systems</i>, vol. 1, no. 3, Elsevier, 2015, pp. P224-237, doi:<a href=\"https://doi.org/10.1016/j.cels.2015.08.012\">10.1016/j.cels.2015.08.012</a>.","short":"A. Ori, B.H. Toyama, M.S. Harris, T. Bock, M. Iskar, P. Bork, N.T. Ingolia, M. Hetzer, M. Beck, Cell Systems 1 (2015) P224-237.","ama":"Ori A, Toyama BH, Harris MS, et al. Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats. <i>Cell Systems</i>. 2015;1(3):P224-237. doi:<a href=\"https://doi.org/10.1016/j.cels.2015.08.012\">10.1016/j.cels.2015.08.012</a>","chicago":"Ori, Alessandro, Brandon H. Toyama, Michael S. Harris, Thomas Bock, Murat Iskar, Peer Bork, Nicholas T. Ingolia, Martin Hetzer, and Martin Beck. “Integrated Transcriptome and Proteome Analyses Reveal Organ-Specific Proteome Deterioration in Old Rats.” <i>Cell Systems</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.cels.2015.08.012\">https://doi.org/10.1016/j.cels.2015.08.012</a>.","ieee":"A. Ori <i>et al.</i>, “Integrated transcriptome and proteome analyses reveal organ-specific proteome deterioration in old rats,” <i>Cell Systems</i>, vol. 1, no. 3. Elsevier, pp. P224-237, 2015."},"scopus_import":"1","issue":"3","day":"23","page":"P224-237","oa_version":"Published Version","publication_status":"published","abstract":[{"lang":"eng","text":"Aging is associated with the decline of protein, cell, and organ function. Here, we use an integrated approach to characterize gene expression, bulk translation, and cell biology in the brains and livers of young and old rats. We identify 468 differences in protein abundance between young and old animals. The majority are a consequence of altered translation output, that is, the combined effect of changes in transcript abundance and translation efficiency. In addition, we identify 130 proteins whose overall abundance remains unchanged but whose sub-cellular localization, phosphorylation state, or splice-form varies. While some protein-level differences appear to be a generic property of the rats’ chronological age, the majority are specific to one organ. These may be a consequence of the organ’s physiology or the chronological age of the cells within the tissue. Taken together, our study provides an initial view of the proteome at the molecular, sub-cellular, and organ level in young and old rats."}],"date_updated":"2022-07-18T08:44:07Z","status":"public","month":"09","publication_identifier":{"issn":["2405-4712"]},"quality_controlled":"1","article_type":"original","volume":1,"date_created":"2022-04-07T07:49:39Z","pmid":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","article_processing_charge":"No","intvolume":"         1","keyword":["Cell Biology","Histology","Pathology and Forensic Medicine"],"author":[{"full_name":"Ori, Alessandro","first_name":"Alessandro","last_name":"Ori"},{"last_name":"Toyama","full_name":"Toyama, Brandon H.","first_name":"Brandon H."},{"full_name":"Harris, Michael S.","first_name":"Michael S.","last_name":"Harris"},{"first_name":"Thomas","full_name":"Bock, Thomas","last_name":"Bock"},{"last_name":"Iskar","full_name":"Iskar, Murat","first_name":"Murat"},{"last_name":"Bork","first_name":"Peer","full_name":"Bork, Peer"},{"last_name":"Ingolia","full_name":"Ingolia, Nicholas T.","first_name":"Nicholas T."},{"full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X"},{"full_name":"Beck, Martin","first_name":"Martin","last_name":"Beck"}],"_id":"11078","oa":1,"date_published":"2015-09-23T00:00:00Z","doi":"10.1016/j.cels.2015.08.012","language":[{"iso":"eng"}],"year":"2015","publisher":"Elsevier","type":"journal_article"},{"article_processing_charge":"No","extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","keyword":["Cell Biology","Genetics","Molecular Medicine"],"intvolume":"        17","date_created":"2022-04-07T07:49:51Z","pmid":1,"article_type":"original","volume":17,"month":"12","quality_controlled":"1","publication_identifier":{"issn":["1934-5909"]},"type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1016/j.stem.2015.09.001","publisher":"Elsevier","year":"2015","date_published":"2015-12-03T00:00:00Z","author":[{"full_name":"Mertens, Jerome","first_name":"Jerome","last_name":"Mertens"},{"full_name":"Paquola, Apuã C.M.","first_name":"Apuã C.M.","last_name":"Paquola"},{"first_name":"Manching","full_name":"Ku, Manching","last_name":"Ku"},{"first_name":"Emily","full_name":"Hatch, Emily","last_name":"Hatch"},{"last_name":"Böhnke","full_name":"Böhnke, Lena","first_name":"Lena"},{"full_name":"Ladjevardi, Shauheen","first_name":"Shauheen","last_name":"Ladjevardi"},{"first_name":"Sean","full_name":"McGrath, Sean","last_name":"McGrath"},{"first_name":"Benjamin","full_name":"Campbell, Benjamin","last_name":"Campbell"},{"last_name":"Lee","full_name":"Lee, Hyungjun","first_name":"Hyungjun"},{"full_name":"Herdy, Joseph R.","first_name":"Joseph R.","last_name":"Herdy"},{"last_name":"Gonçalves","full_name":"Gonçalves, J. Tiago","first_name":"J. Tiago"},{"full_name":"Toda, Tomohisa","first_name":"Tomohisa","last_name":"Toda"},{"last_name":"Kim","first_name":"Yongsung","full_name":"Kim, Yongsung"},{"full_name":"Winkler, Jürgen","first_name":"Jürgen","last_name":"Winkler"},{"last_name":"Yao","first_name":"Jun","full_name":"Yao, Jun"},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","full_name":"HETZER, Martin W","first_name":"Martin W"},{"last_name":"Gage","first_name":"Fred H.","full_name":"Gage, Fred H."}],"oa":1,"_id":"11079","issue":"6","scopus_import":"1","citation":{"apa":"Mertens, J., Paquola, A. C. M., Ku, M., Hatch, E., Böhnke, L., Ladjevardi, S., … Gage, F. H. (2015). Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. <i>Cell Stem Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">https://doi.org/10.1016/j.stem.2015.09.001</a>","ista":"Mertens J, Paquola ACM, Ku M, Hatch E, Böhnke L, Ladjevardi S, McGrath S, Campbell B, Lee H, Herdy JR, Gonçalves JT, Toda T, Kim Y, Winkler J, Yao J, Hetzer M, Gage FH. 2015. Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. Cell Stem Cell. 17(6), 705–718.","mla":"Mertens, Jerome, et al. “Directly Reprogrammed Human Neurons Retain Aging-Associated Transcriptomic Signatures and Reveal Age-Related Nucleocytoplasmic Defects.” <i>Cell Stem Cell</i>, vol. 17, no. 6, Elsevier, 2015, pp. 705–18, doi:<a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">10.1016/j.stem.2015.09.001</a>.","short":"J. Mertens, A.C.M. Paquola, M. Ku, E. Hatch, L. Böhnke, S. Ladjevardi, S. McGrath, B. Campbell, H. Lee, J.R. Herdy, J.T. Gonçalves, T. Toda, Y. Kim, J. Winkler, J. Yao, M. Hetzer, F.H. Gage, Cell Stem Cell 17 (2015) 705–718.","ama":"Mertens J, Paquola ACM, Ku M, et al. Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects. <i>Cell Stem Cell</i>. 2015;17(6):705-718. doi:<a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">10.1016/j.stem.2015.09.001</a>","chicago":"Mertens, Jerome, Apuã C.M. Paquola, Manching Ku, Emily Hatch, Lena Böhnke, Shauheen Ladjevardi, Sean McGrath, et al. “Directly Reprogrammed Human Neurons Retain Aging-Associated Transcriptomic Signatures and Reveal Age-Related Nucleocytoplasmic Defects.” <i>Cell Stem Cell</i>. Elsevier, 2015. <a href=\"https://doi.org/10.1016/j.stem.2015.09.001\">https://doi.org/10.1016/j.stem.2015.09.001</a>.","ieee":"J. Mertens <i>et al.</i>, “Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects,” <i>Cell Stem Cell</i>, vol. 17, no. 6. Elsevier, pp. 705–718, 2015."},"publication":"Cell Stem Cell","external_id":{"pmid":["26456686"]},"title":"Directly reprogrammed human neurons retain aging-associated transcriptomic signatures and reveal age-related nucleocytoplasmic defects","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.stem.2015.09.001"}],"status":"public","date_updated":"2022-07-18T08:44:21Z","page":"705-718","oa_version":"Published Version","publication_status":"published","day":"03","abstract":[{"text":"Aging is a major risk factor for many human diseases, and in vitro generation of human neurons is an attractive approach for modeling aging-related brain disorders. However, modeling aging in differentiated human neurons has proved challenging. We generated neurons from human donors across a broad range of ages, either by iPSC-based reprogramming and differentiation or by direct conversion into induced neurons (iNs). While iPSCs and derived neurons did not retain aging-associated gene signatures, iNs displayed age-specific transcriptional profiles and revealed age-associated decreases in the nuclear transport receptor RanBP17. We detected an age-dependent loss of nucleocytoplasmic compartmentalization (NCC) in donor fibroblasts and corresponding iNs and found that reduced RanBP17 impaired NCC in young cells, while iPSC rejuvenation restored NCC in aged cells. These results show that iNs retain important aging-related signatures, thus allowing modeling of the aging process in vitro, and they identify impaired NCC as an important factor in human aging.","lang":"eng"}]},{"publisher":"Oxford University Press","year":"2015","language":[{"iso":"eng"}],"doi":"10.1093/pcp/pcv087","type":"journal_article","_id":"12196","author":[{"full_name":"Johnson, Kaeli C.M.","first_name":"Kaeli C.M.","last_name":"Johnson"},{"last_name":"Xia","full_name":"Xia, Shitou","first_name":"Shitou"},{"last_name":"Feng","id":"e0164712-22ee-11ed-b12a-d80fcdf35958","orcid":"0000-0002-4008-1234","first_name":"Xiaoqi","full_name":"Feng, Xiaoqi"},{"last_name":"Li","first_name":"Xin","full_name":"Li, Xin"}],"date_published":"2015-08-01T00:00:00Z","pmid":1,"department":[{"_id":"XiFe"}],"acknowledgement":"This work was supported by the National Sciences and Engineering Research Council of Canada [Canada Graduate\r\nScholarship–Doctoral to K.J.; Discovery Grant to X.L.]; the department of Botany at the University of f British Columbia\r\n[the Dewar Cooper Memorial Fund to X.L.].The authors would like to thank Dr. Yuelin Zhang and Ms. Yan Li for their assistance with next-generation sequencing, and Mr. Charles Copeland for critical reading of the manuscript.","date_created":"2023-01-16T09:20:22Z","keyword":["Cell Biology","Plant Science","Physiology","General Medicine"],"intvolume":"        56","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","quality_controlled":"1","publication_identifier":{"issn":["0032-0781","1471-9053"]},"month":"08","article_type":"original","volume":56,"date_updated":"2023-05-08T11:03:23Z","status":"public","abstract":[{"text":"SNC1 (SUPPRESSOR OF NPR1, CONSTITUTIVE 1) is one of a suite of intracellular Arabidopsis NOD-like receptor (NLR) proteins which, upon activation, result in the induction of defense responses. However, the molecular mechanisms underlying NLR activation and the subsequent provocation of immune responses are only partially characterized. To identify negative regulators of NLR-mediated immunity, a forward genetic screen was undertaken to search for enhancers of the dwarf, autoimmune gain-of-function snc1 mutant. To avoid lethality resulting from severe dwarfism, the screen was conducted using mos4 (modifier of snc1, 4) snc1 plants, which display wild-type-like morphology and resistance. M2 progeny were screened for mutant, snc1-enhancing (muse) mutants displaying a reversion to snc1-like phenotypes. The muse9 mos4 snc1 triple mutant was found to exhibit dwarf morphology, elevated expression of the pPR2-GUS defense marker reporter gene and enhanced resistance to the oomycete pathogen Hyaloperonospora arabidopsidis Noco2. Via map-based cloning and Illumina sequencing, it was determined that the muse9 mutation is in the gene encoding the SWI/SNF chromatin remodeler SYD (SPLAYED), and was thus renamed syd-10. The syd-10 single mutant has no observable alteration from wild-type-like resistance, although the syd-4 T-DNA insertion allele displays enhanced resistance to the bacterial pathogen Pseudomonas syringae pv. maculicola ES4326. Transcription of SNC1 is increased in both syd-4 and syd-10. These data suggest that SYD plays a subtle, specific role in the regulation of SNC1 expression and SNC1-mediated immunity. SYD may work with other proteins at the chromatin level to repress SNC1 transcription; such regulation is important for fine-tuning the expression of NLR-encoding genes to prevent unpropitious autoimmunity.","lang":"eng"}],"oa_version":"None","page":"1616-1623","publication_status":"published","citation":{"chicago":"Johnson, Kaeli C.M., Shitou Xia, Xiaoqi Feng, and Xin Li. “The Chromatin Remodeler SPLAYED Negatively Regulates SNC1-Mediated Immunity.” <i>Plant and Cell Physiology</i>. Oxford University Press, 2015. <a href=\"https://doi.org/10.1093/pcp/pcv087\">https://doi.org/10.1093/pcp/pcv087</a>.","ieee":"K. C. M. Johnson, S. Xia, X. Feng, and X. Li, “The chromatin remodeler SPLAYED negatively regulates SNC1-mediated immunity,” <i>Plant and Cell Physiology</i>, vol. 56, no. 8. Oxford University Press, pp. 1616–1623, 2015.","apa":"Johnson, K. C. M., Xia, S., Feng, X., &#38; Li, X. (2015). The chromatin remodeler SPLAYED negatively regulates SNC1-mediated immunity. <i>Plant and Cell Physiology</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/pcp/pcv087\">https://doi.org/10.1093/pcp/pcv087</a>","short":"K.C.M. Johnson, S. Xia, X. Feng, X. Li, Plant and Cell Physiology 56 (2015) 1616–1623.","ista":"Johnson KCM, Xia S, Feng X, Li X. 2015. The chromatin remodeler SPLAYED negatively regulates SNC1-mediated immunity. Plant and Cell Physiology. 56(8), 1616–1623.","mla":"Johnson, Kaeli C. M., et al. “The Chromatin Remodeler SPLAYED Negatively Regulates SNC1-Mediated Immunity.” <i>Plant and Cell Physiology</i>, vol. 56, no. 8, Oxford University Press, 2015, pp. 1616–23, doi:<a href=\"https://doi.org/10.1093/pcp/pcv087\">10.1093/pcp/pcv087</a>.","ama":"Johnson KCM, Xia S, Feng X, Li X. The chromatin remodeler SPLAYED negatively regulates SNC1-mediated immunity. <i>Plant and Cell Physiology</i>. 2015;56(8):1616-1623. doi:<a href=\"https://doi.org/10.1093/pcp/pcv087\">10.1093/pcp/pcv087</a>"},"issue":"8","scopus_import":"1","external_id":{"pmid":["26063389"]},"title":"The chromatin remodeler SPLAYED negatively regulates SNC1-mediated immunity","publication":"Plant and Cell Physiology"},{"date_created":"2022-04-07T07:50:13Z","pmid":1,"extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","intvolume":"       205","keyword":["Cell Biology"],"month":"04","publication_identifier":{"issn":["1540-8140","0021-9525"]},"quality_controlled":"1","volume":205,"article_type":"review","doi":"10.1083/jcb.201402003","language":[{"iso":"eng"}],"year":"2014","publisher":"Rockefeller University Press","type":"journal_article","author":[{"last_name":"Hatch","first_name":"Emily","full_name":"Hatch, Emily"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W"}],"_id":"11081","oa":1,"date_published":"2014-04-21T00:00:00Z","citation":{"ieee":"E. Hatch and M. Hetzer, “Breaching the nuclear envelope in development and disease,” <i>Journal of Cell Biology</i>, vol. 205, no. 2. Rockefeller University Press, pp. 133–141, 2014.","chicago":"Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development and Disease.” <i>Journal of Cell Biology</i>. Rockefeller University Press, 2014. <a href=\"https://doi.org/10.1083/jcb.201402003\">https://doi.org/10.1083/jcb.201402003</a>.","ama":"Hatch E, Hetzer M. Breaching the nuclear envelope in development and disease. <i>Journal of Cell Biology</i>. 2014;205(2):133-141. doi:<a href=\"https://doi.org/10.1083/jcb.201402003\">10.1083/jcb.201402003</a>","apa":"Hatch, E., &#38; Hetzer, M. (2014). Breaching the nuclear envelope in development and disease. <i>Journal of Cell Biology</i>. Rockefeller University Press. <a href=\"https://doi.org/10.1083/jcb.201402003\">https://doi.org/10.1083/jcb.201402003</a>","short":"E. Hatch, M. Hetzer, Journal of Cell Biology 205 (2014) 133–141.","mla":"Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development and Disease.” <i>Journal of Cell Biology</i>, vol. 205, no. 2, Rockefeller University Press, 2014, pp. 133–41, doi:<a href=\"https://doi.org/10.1083/jcb.201402003\">10.1083/jcb.201402003</a>.","ista":"Hatch E, Hetzer M. 2014. Breaching the nuclear envelope in development and disease. Journal of Cell Biology. 205(2), 133–141."},"scopus_import":"1","issue":"2","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1083/jcb.201402003"}],"publication":"Journal of Cell Biology","title":"Breaching the nuclear envelope in development and disease","external_id":{"pmid":["24751535"]},"date_updated":"2022-07-18T08:45:09Z","status":"public","day":"21","oa_version":"Published Version","page":"133-141","publication_status":"published","abstract":[{"lang":"eng","text":"In eukaryotic cells the nuclear genome is enclosed by the nuclear envelope (NE). In metazoans, the NE breaks down in mitosis and it has been assumed that the physical barrier separating nucleoplasm and cytoplasm remains intact during the rest of the cell cycle and cell differentiation. However, recent studies suggest that nonmitotic NE remodeling plays a critical role in development, virus infection, laminopathies, and cancer. Although the mechanisms underlying these NE restructuring events are currently being defined, one common theme is activation of protein kinase C family members in the interphase nucleus to disrupt the nuclear lamina, demonstrating the importance of the lamina in maintaining nuclear integrity."}]},{"volume":25,"article_type":"original","quality_controlled":"1","publication_identifier":{"issn":["1059-1524","1939-4586"]},"month":"08","keyword":["Cell Biology","Molecular Biology"],"intvolume":"        25","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","article_processing_charge":"No","date_created":"2022-04-07T07:50:24Z","date_published":"2014-08-15T00:00:00Z","oa":1,"_id":"11082","author":[{"first_name":"Abigail L.","full_name":"Buchwalter, Abigail L.","last_name":"Buchwalter"},{"last_name":"Liang","full_name":"Liang, Yun","first_name":"Yun"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X","first_name":"Martin W","full_name":"HETZER, Martin W"}],"type":"journal_article","publisher":"American Society for Cell Biology","year":"2014","language":[{"iso":"eng"}],"doi":"10.1091/mbc.e14-04-0865","title":"Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics","publication":"Molecular Biology of the Cell","main_file_link":[{"url":"https://doi.org/10.1091/mbc.e14-04-0865","open_access":"1"}],"issue":"16","scopus_import":"1","citation":{"short":"A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014) 2472–2484.","apa":"Buchwalter, A. L., Liang, Y., &#38; Hetzer, M. (2014). Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. <i>Molecular Biology of the Cell</i>. American Society for Cell Biology. <a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">https://doi.org/10.1091/mbc.e14-04-0865</a>","mla":"Buchwalter, Abigail L., et al. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” <i>Molecular Biology of the Cell</i>, vol. 25, no. 16, American Society for Cell Biology, 2014, pp. 2472–84, doi:<a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">10.1091/mbc.e14-04-0865</a>.","ista":"Buchwalter AL, Liang Y, Hetzer M. 2014. Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. Molecular Biology of the Cell. 25(16), 2472–2484.","ama":"Buchwalter AL, Liang Y, Hetzer M. Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics. <i>Molecular Biology of the Cell</i>. 2014;25(16):2472-2484. doi:<a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">10.1091/mbc.e14-04-0865</a>","chicago":"Buchwalter, Abigail L., Yun Liang, and Martin Hetzer. “Nup50 Is Required for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” <i>Molecular Biology of the Cell</i>. American Society for Cell Biology, 2014. <a href=\"https://doi.org/10.1091/mbc.e14-04-0865\">https://doi.org/10.1091/mbc.e14-04-0865</a>.","ieee":"A. L. Buchwalter, Y. Liang, and M. Hetzer, “Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics,” <i>Molecular Biology of the Cell</i>, vol. 25, no. 16. American Society for Cell Biology, pp. 2472–2484, 2014."},"abstract":[{"text":"The nuclear pore complex (NPC) plays a critical role in gene expression by mediating import of transcription regulators into the nucleus and export of RNA transcripts to the cytoplasm. Emerging evidence suggests that in addition to mediating transport, a subset of nucleoporins (Nups) engage in transcriptional activation and elongation at genomic loci that are not associated with NPCs. The underlying mechanism and regulation of Nup mobility on and off nuclear pores remain unclear. Here we show that Nup50 is a mobile Nup with a pronounced presence both at the NPC and in the nucleoplasm that can move between these different localizations. Strikingly, the dynamic behavior of Nup50 in both locations is dependent on active transcription by RNA polymerase II and requires the N-terminal half of the protein, which contains importin α– and Nup153-binding domains. However, Nup50 dynamics are independent of importin α, Nup153, and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility. Of interest, depletion of Nup50 from C2C12 myoblasts does not affect cell proliferation but inhibits differentiation into myotubes. Taken together, our results suggest a transport-independent role for Nup50 in chromatin biology that occurs away from the NPC.","lang":"eng"}],"publication_status":"published","page":"2472-2484","oa_version":"Published Version","day":"15","status":"public","date_updated":"2022-07-18T08:45:20Z"},{"type":"journal_article","doi":"10.1016/j.tcb.2012.10.013","language":[{"iso":"eng"}],"year":"2013","publisher":"Elsevier","date_published":"2013-03-01T00:00:00Z","author":[{"full_name":"Franks, Tobias M.","first_name":"Tobias M.","last_name":"Franks"},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W"}],"_id":"11083","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","extern":"1","intvolume":"        23","keyword":["Cell Biology"],"date_created":"2022-04-07T07:50:33Z","pmid":1,"volume":23,"article_type":"letter_note","month":"03","publication_identifier":{"issn":["0962-8924"]},"quality_controlled":"1","status":"public","date_updated":"2022-07-18T08:45:34Z","day":"01","publication_status":"published","oa_version":"None","page":"112-117","abstract":[{"text":"Nuclear pore complex (NPC) proteins are known for their critical roles in regulating nucleocytoplasmic traffic of macromolecules across the nuclear envelope. However, recent findings suggest that some nucleoporins (Nups), including Nup98, have additional functions in developmental gene regulation. Nup98, which exhibits transcription-dependent mobility at the NPC but can also bind chromatin away from the nuclear envelope, is frequently involved in chromosomal translocations in a subset of patients suffering from acute myeloid leukemia (AML). A common paradigm suggests that Nup98 translocations cause aberrant transcription when they are recuited to aberrant genomic loci. Importantly, this model fails to account for the potential loss of wild type (WT) Nup98 function in the presence of Nup98 translocation mutants. Here we examine how the cell might regulate Nup98 nucleoplasmic protein levels to control transcription in healthy cells. In addition, we discuss the possibility that dominant negative Nup98 fusion proteins disrupt the transcriptional activity of WT Nup98 in the nucleoplasm to drive AML.","lang":"eng"}],"scopus_import":"1","issue":"3","citation":{"mla":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>, vol. 23, no. 3, Elsevier, 2013, pp. 112–17, doi:<a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">10.1016/j.tcb.2012.10.013</a>.","ista":"Franks TM, Hetzer M. 2013. The role of Nup98 in transcription regulation in healthy and diseased cells. Trends in Cell Biology. 23(3), 112–117.","apa":"Franks, T. M., &#38; Hetzer, M. (2013). The role of Nup98 in transcription regulation in healthy and diseased cells. <i>Trends in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">https://doi.org/10.1016/j.tcb.2012.10.013</a>","short":"T.M. Franks, M. Hetzer, Trends in Cell Biology 23 (2013) 112–117.","ama":"Franks TM, Hetzer M. The role of Nup98 in transcription regulation in healthy and diseased cells. <i>Trends in Cell Biology</i>. 2013;23(3):112-117. doi:<a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">10.1016/j.tcb.2012.10.013</a>","chicago":"Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>. Elsevier, 2013. <a href=\"https://doi.org/10.1016/j.tcb.2012.10.013\">https://doi.org/10.1016/j.tcb.2012.10.013</a>.","ieee":"T. M. Franks and M. Hetzer, “The role of Nup98 in transcription regulation in healthy and diseased cells,” <i>Trends in Cell Biology</i>, vol. 23, no. 3. Elsevier, pp. 112–117, 2013."},"publication":"Trends in Cell Biology","title":"The role of Nup98 in transcription regulation in healthy and diseased cells","external_id":{"pmid":["23246429"]}},{"date_updated":"2022-07-18T08:37:53Z","status":"public","abstract":[{"lang":"eng","text":"Protein turnover is an effective way of maintaining a functional proteome, as old and potentially damaged polypeptides are destroyed and replaced by newly synthesized copies. An increasing number of intracellular proteins, however, have been identified that evade this turnover process and instead are maintained over a cell's lifetime. This diverse group of long-lived proteins might be particularly prone to accumulation of damage and thus have a crucial role in the functional deterioration of key regulatory processes during ageing."}],"page":"55-61","publication_status":"published","oa_version":"None","day":"01","citation":{"ieee":"B. H. Toyama and M. Hetzer, “Protein homeostasis: Live long, won’t prosper,” <i>Nature Reviews Molecular Cell Biology</i>, vol. 14. Springer Nature, pp. 55–61, 2013.","chicago":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” <i>Nature Reviews Molecular Cell Biology</i>. Springer Nature, 2013. <a href=\"https://doi.org/10.1038/nrm3496\">https://doi.org/10.1038/nrm3496</a>.","ama":"Toyama BH, Hetzer M. Protein homeostasis: Live long, won’t prosper. <i>Nature Reviews Molecular Cell Biology</i>. 2013;14:55-61. doi:<a href=\"https://doi.org/10.1038/nrm3496\">10.1038/nrm3496</a>","apa":"Toyama, B. H., &#38; Hetzer, M. (2013). Protein homeostasis: Live long, won’t prosper. <i>Nature Reviews Molecular Cell Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/nrm3496\">https://doi.org/10.1038/nrm3496</a>","short":"B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.","ista":"Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper. Nature Reviews Molecular Cell Biology. 14, 55–61.","mla":"Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t Prosper.” <i>Nature Reviews Molecular Cell Biology</i>, vol. 14, Springer Nature, 2013, pp. 55–61, doi:<a href=\"https://doi.org/10.1038/nrm3496\">10.1038/nrm3496</a>."},"scopus_import":"1","external_id":{"pmid":["23258296"]},"title":"Protein homeostasis: Live long, won't prosper","publication":"Nature Reviews Molecular Cell Biology","publisher":"Springer Nature","year":"2013","language":[{"iso":"eng"}],"doi":"10.1038/nrm3496","type":"journal_article","_id":"11084","author":[{"last_name":"Toyama","full_name":"Toyama, Brandon H.","first_name":"Brandon H."},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W"}],"date_published":"2013-01-01T00:00:00Z","pmid":1,"date_created":"2022-04-07T07:50:43Z","keyword":["Cell Biology","Molecular Biology"],"intvolume":"        14","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","extern":"1","quality_controlled":"1","publication_identifier":{"issn":["1471-0072","1471-0080"]},"month":"01","volume":14,"article_type":"original"},{"doi":"10.1016/j.ceb.2012.08.008","language":[{"iso":"eng"}],"year":"2012","publisher":"Elsevier","type":"journal_article","author":[{"last_name":"Gomez-Cavazos","full_name":"Gomez-Cavazos, J Sebastian","first_name":"J Sebastian"},{"first_name":"Martin W","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","orcid":"0000-0002-2111-992X"}],"_id":"11089","date_published":"2012-12-01T00:00:00Z","date_created":"2022-04-07T07:51:37Z","pmid":1,"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","article_processing_charge":"No","extern":"1","intvolume":"        24","keyword":["Cell Biology"],"month":"12","publication_identifier":{"issn":["0955-0674"]},"quality_controlled":"1","article_type":"original","volume":24,"date_updated":"2022-07-18T08:38:47Z","status":"public","day":"01","publication_status":"published","oa_version":"None","page":"775-783","abstract":[{"lang":"eng","text":"The Nuclear Envelope (NE) contains over 100 different proteins that associate with nuclear components such as chromatin, the lamina and the transcription machinery. Mutations in genes encoding NE proteins have been shown to result in tissue-specific defects and disease, suggesting cell-type specific differences in NE composition and function. Consistent with these observations, recent studies have revealed unexpected functions for numerous NE associated proteins during cell differentiation and development. Here we review the latest insights into the roles played by the NE in cell differentiation, development, disease and aging, focusing primarily on inner nuclear membrane (INM) proteins and nuclear pore components."}],"citation":{"ieee":"J. S. Gomez-Cavazos and M. Hetzer, “Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins,” <i>Current Opinion in Cell Biology</i>, vol. 24, no. 6. Elsevier, pp. 775–783, 2012.","chicago":"Gomez-Cavazos, J Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” <i>Current Opinion in Cell Biology</i>. Elsevier, 2012. <a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">https://doi.org/10.1016/j.ceb.2012.08.008</a>.","ama":"Gomez-Cavazos JS, Hetzer M. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. <i>Current Opinion in Cell Biology</i>. 2012;24(6):775-783. doi:<a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">10.1016/j.ceb.2012.08.008</a>","mla":"Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “Outfits for Different Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” <i>Current Opinion in Cell Biology</i>, vol. 24, no. 6, Elsevier, 2012, pp. 775–83, doi:<a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">10.1016/j.ceb.2012.08.008</a>.","apa":"Gomez-Cavazos, J. S., &#38; Hetzer, M. (2012). Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. <i>Current Opinion in Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ceb.2012.08.008\">https://doi.org/10.1016/j.ceb.2012.08.008</a>","ista":"Gomez-Cavazos JS, Hetzer M. 2012. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. Current Opinion in Cell Biology. 24(6), 775–783.","short":"J.S. Gomez-Cavazos, M. Hetzer, Current Opinion in Cell Biology 24 (2012) 775–783."},"scopus_import":"1","issue":"6","publication":"Current Opinion in Cell Biology","title":"Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins","external_id":{"pmid":["22995343"]}}]