[{"file":[{"relation":"main_file","success":1,"access_level":"open_access","creator":"dernst","file_id":"14941","file_size":9645056,"checksum":"53c3ef43d9bd6d7bff3ffcf57d763cac","date_created":"2024-02-05T12:35:03Z","content_type":"application/pdf","file_name":"2023_EmboReports_PimentaMarques.pdf","date_updated":"2024-02-05T12:35:03Z"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","publication_identifier":{"eissn":["1469-3178"]},"oa":1,"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"type":"journal_article","date_published":"2024-01-10T00:00:00Z","language":[{"iso":"eng"}],"oa_version":"Published Version","month":"01","has_accepted_license":"1","publication":"EMBO reports","volume":25,"acknowledgement":"We thank all members of the Cell Cycle and Regulation Lab for the discussions and for the critical reading of the manuscript. We thank Tomer Avidor-Reiss (University of Toledo, Toledo, OH), Daniel St. Johnston (The Gurdon Institute, Cambridge, UK), David Glover (University of Cambridge, Cambridge, UK), Jingyan Fu (Agricultural University, Beijing, China) Jordan Raff (University of Oxford, Oxford, UK) and Timothy Megraw (Florida State University, Tallahassee, FL) for sharing tools. We acknowledge the technical support of Instituto Gulbenkian de Ciência (IGC)‘s Advanced Imaging Facility, in particular Gabriel Martins, Nuno Pimpão Martins and José Marques. We also thank Tiago Paixão from the IGC’s Quantitative & Digital Science Unit and Marco Louro from the CCR lab for the support provided on statistical analysis. IGC’s Advanced Imaging Facility (AIF-UIC) is supported by the national Portuguese funding ref# PPBI-POCI-01-0145-FEDER -022122. We thank the IGC’s Fly Facility, supported by CONGENTO (LISBOA-01-0145-FEDER-022170). This work was supported by an ERC grant (ERC-2015-CoG-683258) awarded to MBD and a grant from the Portuguese Research Council (FCT) awarded to APM (PTDC/BIA-BID/32225/2017).","ddc":["570"],"day":"10","doi":"10.1038/s44319-023-00020-6","abstract":[{"text":"Centrioles are part of centrosomes and cilia, which are microtubule organising centres (MTOC) with diverse functions. Despite their stability, centrioles can disappear during differentiation, such as in oocytes, but little is known about the regulation of their structural integrity. Our previous research revealed that the pericentriolar material (PCM) that surrounds centrioles and its recruiter, Polo kinase, are downregulated in oogenesis and sufficient for maintaining both centrosome structural integrity and MTOC activity. We now show that the expression of specific components of the centriole cartwheel and wall, including ANA1/CEP295, is essential for maintaining centrosome integrity. We find that Polo kinase requires ANA1 to promote centriole stability in cultured cells and eggs. In addition, ANA1 expression prevents the loss of centrioles observed upon PCM-downregulation. However, the centrioles maintained by overexpressing and tethering ANA1 are inactive, unlike the MTOCs observed upon tethering Polo kinase. These findings demonstrate that several centriole components are needed to maintain centrosome structure. Our study also highlights that centrioles are more dynamic than previously believed, with their structural stability relying on the continuous expression of multiple components.","lang":"eng"}],"citation":{"short":"A. Pimenta-Marques, T. Perestrelo, P. Dos Reis Rodrigues, P. Duarte, A. Ferreira-Silva, M. Lince-Faria, M. Bettencourt-Dias, EMBO Reports 25 (2024) 102–127.","mla":"Pimenta-Marques, Ana, et al. “Ana1/CEP295 Is an Essential Player in the Centrosome Maintenance Program Regulated by Polo Kinase and the PCM.” <i>EMBO Reports</i>, vol. 25, no. 1, Embo Press, 2024, pp. 102–27, doi:<a href=\"https://doi.org/10.1038/s44319-023-00020-6\">10.1038/s44319-023-00020-6</a>.","ista":"Pimenta-Marques A, Perestrelo T, Dos Reis Rodrigues P, Duarte P, Ferreira-Silva A, Lince-Faria M, Bettencourt-Dias M. 2024. Ana1/CEP295 is an essential player in the centrosome maintenance program regulated by Polo kinase and the PCM. EMBO reports. 25(1), 102–127.","apa":"Pimenta-Marques, A., Perestrelo, T., Dos Reis Rodrigues, P., Duarte, P., Ferreira-Silva, A., Lince-Faria, M., &#38; Bettencourt-Dias, M. (2024). Ana1/CEP295 is an essential player in the centrosome maintenance program regulated by Polo kinase and the PCM. <i>EMBO Reports</i>. Embo Press. <a href=\"https://doi.org/10.1038/s44319-023-00020-6\">https://doi.org/10.1038/s44319-023-00020-6</a>","ama":"Pimenta-Marques A, Perestrelo T, Dos Reis Rodrigues P, et al. Ana1/CEP295 is an essential player in the centrosome maintenance program regulated by Polo kinase and the PCM. <i>EMBO reports</i>. 2024;25(1):102-127. doi:<a href=\"https://doi.org/10.1038/s44319-023-00020-6\">10.1038/s44319-023-00020-6</a>","chicago":"Pimenta-Marques, Ana, Tania Perestrelo, Patricia Dos Reis Rodrigues, Paulo Duarte, Ana Ferreira-Silva, Mariana Lince-Faria, and Mónica Bettencourt-Dias. “Ana1/CEP295 Is an Essential Player in the Centrosome Maintenance Program Regulated by Polo Kinase and the PCM.” <i>EMBO Reports</i>. Embo Press, 2024. <a href=\"https://doi.org/10.1038/s44319-023-00020-6\">https://doi.org/10.1038/s44319-023-00020-6</a>.","ieee":"A. Pimenta-Marques <i>et al.</i>, “Ana1/CEP295 is an essential player in the centrosome maintenance program regulated by Polo kinase and the PCM,” <i>EMBO reports</i>, vol. 25, no. 1. Embo Press, pp. 102–127, 2024."},"year":"2024","date_updated":"2024-02-05T12:37:07Z","publisher":"Embo Press","article_type":"original","quality_controlled":"1","page":"102-127","file_date_updated":"2024-02-05T12:35:03Z","article_processing_charge":"Yes (in subscription journal)","department":[{"_id":"MiSi"}],"date_created":"2024-02-04T23:00:53Z","publication_status":"published","intvolume":"        25","title":"Ana1/CEP295 is an essential player in the centrosome maintenance program regulated by Polo kinase and the PCM","scopus_import":"1","_id":"14933","issue":"1","author":[{"full_name":"Pimenta-Marques, Ana","last_name":"Pimenta-Marques","first_name":"Ana"},{"last_name":"Perestrelo","first_name":"Tania","full_name":"Perestrelo, Tania"},{"full_name":"Dos Reis Rodrigues, Patricia","orcid":"0000-0003-1681-508X","last_name":"Dos Reis Rodrigues","first_name":"Patricia","id":"26E95904-5160-11E9-9C0B-C5B0DC97E90F"},{"full_name":"Duarte, Paulo","last_name":"Duarte","first_name":"Paulo"},{"last_name":"Ferreira-Silva","first_name":"Ana","full_name":"Ferreira-Silva, Ana"},{"last_name":"Lince-Faria","first_name":"Mariana","full_name":"Lince-Faria, Mariana"},{"first_name":"Mónica","last_name":"Bettencourt-Dias","full_name":"Bettencourt-Dias, Mónica"}]},{"oa_version":"Published Version","month":"07","article_number":"e54163","publication":"EMBO Reports","has_accepted_license":"1","language":[{"iso":"eng"}],"keyword":["Genetics","Molecular Biology","Biochemistry"],"publication_identifier":{"eissn":["1469-3178"],"issn":["1469-221X"]},"oa":1,"date_published":"2022-07-05T00:00:00Z","type":"journal_article","main_file_link":[{"url":"https://doi.org/10.15252/embr.202154163","open_access":"1"}],"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"published","date_created":"2023-01-16T10:01:44Z","article_processing_charge":"No","department":[{"_id":"MaDe"}],"title":"Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning","intvolume":"        23","pmid":1,"_id":"12275","scopus_import":"1","author":[{"first_name":"Maisha","last_name":"Rahman","full_name":"Rahman, Maisha"},{"id":"39831956-E4FE-11E9-85DE-0DC7E5697425","full_name":"Ramirez, Nelson","first_name":"Nelson","last_name":"Ramirez"},{"last_name":"Diaz‐Balzac","first_name":"Carlos A","full_name":"Diaz‐Balzac, Carlos A"},{"first_name":"Hannes E","last_name":"Bülow","full_name":"Bülow, Hannes E"}],"issue":"7","publisher":"Embo Press","article_type":"original","quality_controlled":"1","doi":"10.15252/embr.202154163","day":"05","abstract":[{"lang":"eng","text":"N-glycans are molecularly diverse sugars borne by over 70% of proteins transiting the secretory pathway and have been implicated in protein folding, stability, and localization. Mutations in genes important for N-glycosylation result in congenital disorders of glycosylation that are often associated with intellectual disability. Here, we show that structurally distinct N-glycans regulate an extracellular protein complex involved in the patterning of somatosensory dendrites in Caenorhabditis elegans. Specifically, aman-2/Golgi alpha-mannosidase II, a conserved key enzyme in the biosynthesis of specific N-glycans, regulates the activity of the Menorin adhesion complex without obviously affecting the protein stability and localization of its components. AMAN-2 functions cell-autonomously to allow for decoration of the neuronal transmembrane receptor DMA-1/LRR-TM with the correct set of high-mannose/hybrid/paucimannose N-glycans. Moreover, distinct types of N-glycans on specific N-glycosylation sites regulate DMA-1/LRR-TM receptor function, which, together with three other extracellular proteins, forms the Menorin adhesion complex. In summary, specific N-glycan structures regulate dendrite patterning by coordinating the activity of an extracellular adhesion complex, suggesting that the molecular diversity of N-glycans can contribute to developmental specificity in the nervous system."}],"date_updated":"2023-10-03T11:25:54Z","citation":{"apa":"Rahman, M., Ramirez, N., Diaz‐Balzac, C. A., &#38; Bülow, H. E. (2022). Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning. <i>EMBO Reports</i>. Embo Press. <a href=\"https://doi.org/10.15252/embr.202154163\">https://doi.org/10.15252/embr.202154163</a>","ama":"Rahman M, Ramirez N, Diaz‐Balzac CA, Bülow HE. Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning. <i>EMBO Reports</i>. 2022;23(7). doi:<a href=\"https://doi.org/10.15252/embr.202154163\">10.15252/embr.202154163</a>","ieee":"M. Rahman, N. Ramirez, C. A. Diaz‐Balzac, and H. E. Bülow, “Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning,” <i>EMBO Reports</i>, vol. 23, no. 7. Embo Press, 2022.","chicago":"Rahman, Maisha, Nelson Ramirez, Carlos A Diaz‐Balzac, and Hannes E Bülow. “Specific N-Glycans Regulate an Extracellular Adhesion Complex during Somatosensory Dendrite Patterning.” <i>EMBO Reports</i>. Embo Press, 2022. <a href=\"https://doi.org/10.15252/embr.202154163\">https://doi.org/10.15252/embr.202154163</a>.","short":"M. Rahman, N. Ramirez, C.A. Diaz‐Balzac, H.E. Bülow, EMBO Reports 23 (2022).","mla":"Rahman, Maisha, et al. “Specific N-Glycans Regulate an Extracellular Adhesion Complex during Somatosensory Dendrite Patterning.” <i>EMBO Reports</i>, vol. 23, no. 7, e54163, Embo Press, 2022, doi:<a href=\"https://doi.org/10.15252/embr.202154163\">10.15252/embr.202154163</a>.","ista":"Rahman M, Ramirez N, Diaz‐Balzac CA, Bülow HE. 2022. Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning. EMBO Reports. 23(7), e54163."},"year":"2022","isi":1,"external_id":{"pmid":["35586945"],"isi":["000797302700001"]},"volume":23,"acknowledgement":"We thank Scott Garforth, Sarah Garrett, Peri Kurshan, Yehuda Salzberg, PamelaStanley, Robert Townley, and members of the B€ulow laboratory for commentson the manuscript or helpful discussions during the course of this work. Wethank David Miller, Shohei Mitani, Kang Shen, and Iain Wilson for reagents,and Yuji Kohara for theyk11g705cDNA clone. We are grateful to MeeraTrivedi for sharing thedzIs117strain prior to publication. Some strains wereprovided by the Caenorhabditis Genome Center (funded by the NIH Office ofResearch Infrastructure Programs P40OD010440). This work was supportedby grants from the National Institute of Health (NIH): R01NS096672andR21NS111145to HEB; F31NS100370to MR; T32GM007288and F31HD066967to CADB; P30HD071593to Albert Einstein College of Medicine. We acknowl-edge support to MR by the Department of Neuroscience. NJRS was the recipi-ent of a Colciencias-Fulbright Fellowship and HEB of an Irma T. Hirschl/Monique Weill-Caulier research fellowship"},{"file_date_updated":"2022-05-16T07:07:41Z","quality_controlled":"1","article_type":"original","publisher":"EMBO Press","author":[{"first_name":"Leonardo","last_name":"Restivo","full_name":"Restivo, Leonardo"},{"full_name":"Gerlach, Björn","last_name":"Gerlach","first_name":"Björn"},{"first_name":"Michael","last_name":"Tsoory","full_name":"Tsoory, Michael"},{"full_name":"Bikovski, Lior","first_name":"Lior","last_name":"Bikovski"},{"last_name":"Badurek","first_name":"Sylvia","full_name":"Badurek, Sylvia"},{"last_name":"Pitzer","first_name":"Claudia","full_name":"Pitzer, Claudia"},{"first_name":"Isabelle C.","last_name":"Kos-Braun","full_name":"Kos-Braun, Isabelle C."},{"last_name":"Mausset-Bonnefont","first_name":"Anne Laure Mj","full_name":"Mausset-Bonnefont, Anne Laure Mj"},{"first_name":"Jonathan","last_name":"Ward","full_name":"Ward, Jonathan"},{"last_name":"Schunn","first_name":"Michael","full_name":"Schunn, Michael","orcid":"0000-0003-4326-5300","id":"4272DB4A-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Lucas P.J.J.","last_name":"Noldus","full_name":"Noldus, Lucas P.J.J."},{"first_name":"Anton","last_name":"Bespalov","full_name":"Bespalov, Anton"},{"first_name":"Vootele","last_name":"Voikar","full_name":"Voikar, Vootele"}],"_id":"10283","scopus_import":"1","title":"Towards best practices in research: Role of academic core facilities","intvolume":"        22","publication_status":"published","date_created":"2021-11-14T23:01:24Z","article_processing_charge":"Yes (in subscription journal)","department":[{"_id":"PreCl"}],"ddc":["570"],"acknowledgement":"This EQIPD project has received funding from the Innovative Medicines Initiative 2 Joint Undertaking under grant agreement no. 777364. This Joint Undertaking receives support from the European Union’s Horizon 2020 research and innovation program and EFPIA. LR was supported by the Faculty of Biology and Medicine, University of Lausanne. VV was supported by Biocenter Finland and the Jane and Aatos Erkko Foundation. CP and IKB received funding from the Federal Ministry of Education and Research (BMBF, grant 01PW18001). SB from the Vienna BioCenter Core Facilities (VBCF) Preclinical Phenotyping Facility acknowledges funding from the Austrian Federal Ministry of Education, Science & Research; and the City of Vienna. MT is an incumbent of the Carolito Stiftung Research Fellow Chair in Neurodegenerative Diseases. We thank Dr. Katja Kivinen (Helsinki Institute of Life Science) for discussions and feedback.","volume":22,"isi":1,"external_id":{"isi":["000714350000001"]},"date_updated":"2023-08-14T11:47:35Z","citation":{"apa":"Restivo, L., Gerlach, B., Tsoory, M., Bikovski, L., Badurek, S., Pitzer, C., … Voikar, V. (2021). Towards best practices in research: Role of academic core facilities. <i>EMBO Reports</i>. EMBO Press. <a href=\"https://doi.org/10.15252/embr.202153824\">https://doi.org/10.15252/embr.202153824</a>","ama":"Restivo L, Gerlach B, Tsoory M, et al. Towards best practices in research: Role of academic core facilities. <i>EMBO Reports</i>. 2021;22. doi:<a href=\"https://doi.org/10.15252/embr.202153824\">10.15252/embr.202153824</a>","chicago":"Restivo, Leonardo, Björn Gerlach, Michael Tsoory, Lior Bikovski, Sylvia Badurek, Claudia Pitzer, Isabelle C. Kos-Braun, et al. “Towards Best Practices in Research: Role of Academic Core Facilities.” <i>EMBO Reports</i>. EMBO Press, 2021. <a href=\"https://doi.org/10.15252/embr.202153824\">https://doi.org/10.15252/embr.202153824</a>.","ieee":"L. Restivo <i>et al.</i>, “Towards best practices in research: Role of academic core facilities,” <i>EMBO Reports</i>, vol. 22. EMBO Press, 2021.","short":"L. Restivo, B. Gerlach, M. Tsoory, L. Bikovski, S. Badurek, C. Pitzer, I.C. Kos-Braun, A.L.M. Mausset-Bonnefont, J. Ward, M. Schunn, L.P.J.J. Noldus, A. Bespalov, V. Voikar, EMBO Reports 22 (2021).","mla":"Restivo, Leonardo, et al. “Towards Best Practices in Research: Role of Academic Core Facilities.” <i>EMBO Reports</i>, vol. 22, e53824, EMBO Press, 2021, doi:<a href=\"https://doi.org/10.15252/embr.202153824\">10.15252/embr.202153824</a>.","ista":"Restivo L, Gerlach B, Tsoory M, Bikovski L, Badurek S, Pitzer C, Kos-Braun IC, Mausset-Bonnefont ALM, Ward J, Schunn M, Noldus LPJJ, Bespalov A, Voikar V. 2021. Towards best practices in research: Role of academic core facilities. EMBO Reports. 22, e53824."},"year":"2021","abstract":[{"lang":"eng","text":"During the past decade, the scientific community and outside observers have noted a concerning lack of rigor and transparency in preclinical research that led to talk of a “reproducibility crisis” in the life sciences (Baker, 2016; Bespalov & Steckler, 2018; Heddleston et al, 2021). Various measures have been proposed to address the problem: from better training of scientists to more oversight to expanded publishing practices such as preregistration of studies. The recently published EQIPD (Enhancing Quality in Preclinical Data) System is, to date, the largest initiative that aims to establish a systematic approach for increasing the robustness and reliability of biomedical research (Bespalov et al, 2021). However, promoting a cultural change in research practices warrants a broad adoption of the Quality System and its underlying philosophy. It is here that academic Core Facilities (CF), research service providers at universities and research institutions, can make a difference. It is fair to assume that a significant fraction of published data originated from experiments that were designed, run, or analyzed in CFs. These academic services play an important role in the research ecosystem by offering access to cutting-edge equipment and by developing and testing novel techniques and methods that impact research in the academic and private sectors alike (Bikovski et al, 2020). Equipment and infrastructure are not the only value: CFs employ competent personnel with profound knowledge and practical experience of the specific field of interest: animal behavior, imaging, crystallography, genomics, and so on. Thus, CFs are optimally positioned to address concerns about the quality and robustness of preclinical research."}],"doi":"10.15252/embr.202153824","day":"04","language":[{"iso":"eng"}],"publication":"EMBO Reports","has_accepted_license":"1","month":"11","article_number":"e53824","oa_version":"Published Version","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","status":"public","file":[{"creator":"dernst","file_id":"11381","access_level":"open_access","relation":"main_file","success":1,"file_name":"2021_EmboReports_Restivo.pdf","content_type":"application/pdf","date_updated":"2022-05-16T07:07:41Z","checksum":"74743baa6ef431ef60c3de3bc4da045a","file_size":488583,"date_created":"2022-05-16T07:07:41Z"}],"date_published":"2021-11-04T00:00:00Z","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"oa":1,"publication_identifier":{"issn":["1469-221X"],"eissn":["1469-3178"]}},{"scopus_import":"1","_id":"9913","pmid":1,"issue":"9","author":[{"first_name":"Andrea","last_name":"Vega","full_name":"Vega, Andrea"},{"first_name":"Isabel","last_name":"Fredes","full_name":"Fredes, Isabel"},{"full_name":"O’Brien, José","last_name":"O’Brien","first_name":"José"},{"last_name":"Shen","first_name":"Zhouxin","full_name":"Shen, Zhouxin"},{"full_name":"Ötvös, Krisztina","orcid":"0000-0002-5503-4983","last_name":"Ötvös","first_name":"Krisztina","id":"29B901B0-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Abualia","first_name":"Rashed","full_name":"Abualia, Rashed","orcid":"0000-0002-9357-9415","id":"4827E134-F248-11E8-B48F-1D18A9856A87"},{"orcid":"0000-0002-8510-9739","full_name":"Benková, Eva","first_name":"Eva","last_name":"Benková","id":"38F4F166-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Briggs","first_name":"Steven P.","full_name":"Briggs, Steven P."},{"full_name":"Gutiérrez, Rodrigo A.","first_name":"Rodrigo A.","last_name":"Gutiérrez"}],"department":[{"_id":"EvBe"},{"_id":"GradSch"}],"article_processing_charge":"Yes","date_created":"2021-08-15T22:01:30Z","publication_status":"published","intvolume":"        22","title":"Nitrate triggered phosphoproteome changes and a PIN2 phosphosite modulating root system architecture","quality_controlled":"1","file_date_updated":"2021-10-05T13:36:42Z","publisher":"Wiley","article_type":"original","year":"2021","citation":{"apa":"Vega, A., Fredes, I., O’Brien, J., Shen, Z., Ötvös, K., Abualia, R., … Gutiérrez, R. A. (2021). Nitrate triggered phosphoproteome changes and a PIN2 phosphosite modulating root system architecture. <i>EMBO Reports</i>. Wiley. <a href=\"https://doi.org/10.15252/embr.202051813\">https://doi.org/10.15252/embr.202051813</a>","ama":"Vega A, Fredes I, O’Brien J, et al. Nitrate triggered phosphoproteome changes and a PIN2 phosphosite modulating root system architecture. <i>EMBO Reports</i>. 2021;22(9). doi:<a href=\"https://doi.org/10.15252/embr.202051813\">10.15252/embr.202051813</a>","ieee":"A. Vega <i>et al.</i>, “Nitrate triggered phosphoproteome changes and a PIN2 phosphosite modulating root system architecture,” <i>EMBO Reports</i>, vol. 22, no. 9. Wiley, 2021.","chicago":"Vega, Andrea, Isabel Fredes, José O’Brien, Zhouxin Shen, Krisztina Ötvös, Rashed Abualia, Eva Benková, Steven P. Briggs, and Rodrigo A. Gutiérrez. “Nitrate Triggered Phosphoproteome Changes and a PIN2 Phosphosite Modulating Root System Architecture.” <i>EMBO Reports</i>. Wiley, 2021. <a href=\"https://doi.org/10.15252/embr.202051813\">https://doi.org/10.15252/embr.202051813</a>.","mla":"Vega, Andrea, et al. “Nitrate Triggered Phosphoproteome Changes and a PIN2 Phosphosite Modulating Root System Architecture.” <i>EMBO Reports</i>, vol. 22, no. 9, e51813, Wiley, 2021, doi:<a href=\"https://doi.org/10.15252/embr.202051813\">10.15252/embr.202051813</a>.","short":"A. Vega, I. Fredes, J. O’Brien, Z. Shen, K. Ötvös, R. Abualia, E. Benková, S.P. Briggs, R.A. Gutiérrez, EMBO Reports 22 (2021).","ista":"Vega A, Fredes I, O’Brien J, Shen Z, Ötvös K, Abualia R, Benková E, Briggs SP, Gutiérrez RA. 2021. Nitrate triggered phosphoproteome changes and a PIN2 phosphosite modulating root system architecture. EMBO Reports. 22(9), e51813."},"date_updated":"2024-03-25T23:30:22Z","external_id":{"isi":["000681754200001"],"pmid":["34357701 "]},"isi":1,"day":"06","doi":"10.15252/embr.202051813","abstract":[{"text":"Nitrate commands genome-wide gene expression changes that impact metabolism, physiology, plant growth, and development. In an effort to identify new components involved in nitrate responses in plants, we analyze the Arabidopsis thaliana root phosphoproteome in response to nitrate treatments via liquid chromatography coupled to tandem mass spectrometry. 176 phosphoproteins show significant changes at 5 or 20 min after nitrate treatments. Proteins identified by 5 min include signaling components such as kinases or transcription factors. In contrast, by 20 min, proteins identified were associated with transporter activity or hormone metabolism functions, among others. The phosphorylation profile of NITRATE TRANSPORTER 1.1 (NRT1.1) mutant plants was significantly altered as compared to wild-type plants, confirming its key role in nitrate signaling pathways that involves phosphorylation changes. Integrative bioinformatics analysis highlights auxin transport as an important mechanism modulated by nitrate signaling at the post-translational level. We validated a new phosphorylation site in PIN2 and provide evidence that it functions in primary and lateral root growth responses to nitrate.","lang":"eng"}],"acknowledgement":"This work was supported by ANID—Millennium Science Initiative Program—ICN17_022, Fondo de Desarrollo de Areas Prioritarias (FONDAP) Center for Genome Regulation (15090007), ANID—Fondo Nacional de Desarrollo Científico y Tecnológico (FONDECYT) 1180759 (to RAG) and 1171631 (to AV). We would like to thank Unidad de Microscopía Avanzada UC (UMA UC).","volume":22,"ddc":["580"],"has_accepted_license":"1","publication":"EMBO Reports","oa_version":"Published Version","article_number":"e51813","month":"09","language":[{"iso":"eng"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"type":"journal_article","date_published":"2021-09-06T00:00:00Z","publication_identifier":{"issn":["1469-221X"],"eissn":["1469-3178"]},"oa":1,"file":[{"date_created":"2021-10-05T13:36:42Z","checksum":"750de03dc3b715c37090126c1548ba13","file_size":3144854,"date_updated":"2021-10-05T13:36:42Z","file_name":"2021_EmboR_Vega.pdf","content_type":"application/pdf","access_level":"open_access","success":1,"relation":"main_file","file_id":"10090","creator":"cchlebak"}],"status":"public","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","related_material":{"record":[{"id":"10303","relation":"dissertation_contains","status":"public"}]}},{"has_accepted_license":"1","publication":"EMBO reports","oa_version":"Published Version","article_number":"e45836","month":"09","language":[{"iso":"eng"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"type":"journal_article","date_published":"2018-09-01T00:00:00Z","publication_identifier":{"eissn":["1469-3178"],"issn":["1469-221X"]},"oa":1,"file":[{"access_level":"open_access","relation":"main_file","creator":"kschuh","file_id":"6500","file_size":2005572,"checksum":"6ec90abc637f09cca3a7b6424d7e7a26","date_created":"2019-05-28T13:17:19Z","content_type":"application/pdf","file_name":"2018_embo_Truckenbrodt.pdf","date_updated":"2020-07-14T12:47:32Z"}],"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","status":"public","scopus_import":"1","_id":"6499","issue":"9","author":[{"full_name":"Truckenbrodt, Sven M","first_name":"Sven M","last_name":"Truckenbrodt","id":"45812BD4-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Maidorn, Manuel","first_name":"Manuel","last_name":"Maidorn"},{"full_name":"Crzan, Dagmar","last_name":"Crzan","first_name":"Dagmar"},{"first_name":"Hanna","last_name":"Wildhagen","full_name":"Wildhagen, Hanna"},{"full_name":"Kabatas, Selda","last_name":"Kabatas","first_name":"Selda"},{"full_name":"Rizzoli, Silvio O","first_name":"Silvio O","last_name":"Rizzoli"}],"department":[{"_id":"JoDa"}],"date_created":"2019-05-28T13:16:08Z","article_processing_charge":"No","publication_status":"published","intvolume":"        19","title":"X10 expansion microscopy enables 25‐nm resolution on conventional microscopes","quality_controlled":"1","file_date_updated":"2020-07-14T12:47:32Z","publisher":"EMBO","citation":{"chicago":"Truckenbrodt, Sven M, Manuel Maidorn, Dagmar Crzan, Hanna Wildhagen, Selda Kabatas, and Silvio O Rizzoli. “X10 Expansion Microscopy Enables 25‐nm Resolution on Conventional Microscopes.” <i>EMBO Reports</i>. EMBO, 2018. <a href=\"https://doi.org/10.15252/embr.201845836\">https://doi.org/10.15252/embr.201845836</a>.","ieee":"S. M. Truckenbrodt, M. Maidorn, D. Crzan, H. Wildhagen, S. Kabatas, and S. O. Rizzoli, “X10 expansion microscopy enables 25‐nm resolution on conventional microscopes,” <i>EMBO reports</i>, vol. 19, no. 9. EMBO, 2018.","apa":"Truckenbrodt, S. M., Maidorn, M., Crzan, D., Wildhagen, H., Kabatas, S., &#38; Rizzoli, S. O. (2018). X10 expansion microscopy enables 25‐nm resolution on conventional microscopes. <i>EMBO Reports</i>. EMBO. <a href=\"https://doi.org/10.15252/embr.201845836\">https://doi.org/10.15252/embr.201845836</a>","ama":"Truckenbrodt SM, Maidorn M, Crzan D, Wildhagen H, Kabatas S, Rizzoli SO. X10 expansion microscopy enables 25‐nm resolution on conventional microscopes. <i>EMBO reports</i>. 2018;19(9). doi:<a href=\"https://doi.org/10.15252/embr.201845836\">10.15252/embr.201845836</a>","ista":"Truckenbrodt SM, Maidorn M, Crzan D, Wildhagen H, Kabatas S, Rizzoli SO. 2018. X10 expansion microscopy enables 25‐nm resolution on conventional microscopes. EMBO reports. 19(9), e45836.","short":"S.M. Truckenbrodt, M. Maidorn, D. Crzan, H. Wildhagen, S. Kabatas, S.O. Rizzoli, EMBO Reports 19 (2018).","mla":"Truckenbrodt, Sven M., et al. “X10 Expansion Microscopy Enables 25‐nm Resolution on Conventional Microscopes.” <i>EMBO Reports</i>, vol. 19, no. 9, e45836, EMBO, 2018, doi:<a href=\"https://doi.org/10.15252/embr.201845836\">10.15252/embr.201845836</a>."},"year":"2018","date_updated":"2023-09-19T14:52:32Z","external_id":{"isi":["000443682200009"]},"isi":1,"day":"01","doi":"10.15252/embr.201845836","abstract":[{"lang":"eng","text":"Expansion microscopy is a recently introduced imaging technique that achieves super‐resolution through physically expanding the specimen by ~4×, after embedding into a swellable gel. The resolution attained is, correspondingly, approximately fourfold better than the diffraction limit, or ~70 nm. This is a major improvement over conventional microscopy, but still lags behind modern STED or STORM setups, whose resolution can reach 20–30 nm. We addressed this issue here by introducing an improved gel recipe that enables an expansion factor of ~10× in each dimension, which corresponds to an expansion of the sample volume by more than 1,000‐fold. Our protocol, which we termed X10 microscopy, achieves a resolution of 25–30 nm on conventional epifluorescence microscopes. X10 provides multi‐color images similar or even superior to those produced with more challenging methods, such as STED, STORM, and iterative expansion microscopy (iExM). X10 is therefore the cheapest and easiest option for high‐quality super‐resolution imaging currently available. X10 should be usable in any laboratory, irrespective of the machinery owned or of the technical knowledge."}],"volume":19,"ddc":["580"]},{"pmid":1,"_id":"11105","scopus_import":"1","author":[{"last_name":"Capelson","first_name":"Maya","full_name":"Capelson, Maya"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W","orcid":"0000-0002-2111-992X"}],"issue":"7","publication_status":"published","date_created":"2022-04-07T07:54:06Z","article_processing_charge":"No","title":"The role of nuclear pores in gene regulation, development and disease","intvolume":"        10","page":"697-705","quality_controlled":"1","publisher":"EMBO","article_type":"original","date_updated":"2022-07-18T08:42:44Z","citation":{"chicago":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” <i>EMBO Reports</i>. EMBO, 2009. <a href=\"https://doi.org/10.1038/embor.2009.147\">https://doi.org/10.1038/embor.2009.147</a>.","ieee":"M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation, development and disease,” <i>EMBO reports</i>, vol. 10, no. 7. EMBO, pp. 697–705, 2009.","ama":"Capelson M, Hetzer M. The role of nuclear pores in gene regulation, development and disease. <i>EMBO reports</i>. 2009;10(7):697-705. doi:<a href=\"https://doi.org/10.1038/embor.2009.147\">10.1038/embor.2009.147</a>","apa":"Capelson, M., &#38; Hetzer, M. (2009). The role of nuclear pores in gene regulation, development and disease. <i>EMBO Reports</i>. EMBO. <a href=\"https://doi.org/10.1038/embor.2009.147\">https://doi.org/10.1038/embor.2009.147</a>","ista":"Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation, development and disease. EMBO reports. 10(7), 697–705.","short":"M. Capelson, M. Hetzer, EMBO Reports 10 (2009) 697–705.","mla":"Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation, Development and Disease.” <i>EMBO Reports</i>, vol. 10, no. 7, EMBO, 2009, pp. 697–705, doi:<a href=\"https://doi.org/10.1038/embor.2009.147\">10.1038/embor.2009.147</a>."},"year":"2009","external_id":{"pmid":["19543230"]},"doi":"10.1038/embor.2009.147","day":"01","abstract":[{"text":"Nuclear-pore complexes (NPCs) are large protein channels that span the nuclear envelope (NE), which is a double membrane that encloses the nuclear genome of eukaryotes. Each of the typically 2,000–4,000 pores in the NE of vertebrate cells is composed of multiple copies of 30 different proteins known as nucleoporins. The evolutionarily conserved NPC proteins have the well-characterized function of mediating the transport of molecules between the nucleoplasm and the cytoplasm. Mutations in nucleoporins are often linked to specific developmental defects and disease, and the resulting phenotypes are usually interpreted as the consequences of perturbed nuclear transport activity. However, recent evidence suggests that NPCs have additional functions in chromatin organization and gene regulation, some of which might be independent of nuclear transport. Here, we review the transport-dependent and transport-independent roles of NPCs in the regulation of nuclear function and gene expression.","lang":"eng"}],"volume":10,"extern":"1","publication":"EMBO reports","oa_version":"Published Version","month":"07","language":[{"iso":"eng"}],"keyword":["Genetics","Molecular Biology","Biochemistry"],"date_published":"2009-07-01T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["1469-221X"],"eissn":["1469-3178"]},"oa":1,"main_file_link":[{"url":"https://doi.org/10.1038/embor.2009.147","open_access":"1"}],"status":"public","related_material":{"link":[{"url":"https://doi.org/10.1038/embor.2009.176","relation":"erratum"}]},"user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"publication":"EMBO reports","month":"01","oa_version":"Published Version","keyword":["Genetics","Molecular Biology","Biochemistry"],"language":[{"iso":"eng"}],"type":"journal_article","date_published":"2007-01-19T00:00:00Z","oa":1,"publication_identifier":{"issn":["1469-221X"],"eissn":["1469-3178"]},"status":"public","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","main_file_link":[{"url":"https://doi.org/10.1038/sj.embor.7400889","open_access":"1"}],"issue":"2","author":[{"full_name":"Franz, Cerstin","first_name":"Cerstin","last_name":"Franz"},{"full_name":"Walczak, Rudolf","last_name":"Walczak","first_name":"Rudolf"},{"last_name":"Yavuz","first_name":"Sevil","full_name":"Yavuz, Sevil"},{"full_name":"Santarella, Rachel","first_name":"Rachel","last_name":"Santarella"},{"last_name":"Gentzel","first_name":"Marc","full_name":"Gentzel, Marc"},{"last_name":"Askjaer","first_name":"Peter","full_name":"Askjaer, Peter"},{"full_name":"Galy, Vincent","last_name":"Galy","first_name":"Vincent"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"},{"full_name":"Mattaj, Iain W","first_name":"Iain W","last_name":"Mattaj"},{"full_name":"Antonin, Wolfram","first_name":"Wolfram","last_name":"Antonin"}],"scopus_import":"1","pmid":1,"_id":"11116","intvolume":"         8","title":"MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly","article_processing_charge":"No","date_created":"2022-04-07T07:56:13Z","publication_status":"published","quality_controlled":"1","page":"165-172","article_type":"original","publisher":"EMBO","external_id":{"pmid":["17235358"]},"year":"2007","citation":{"mla":"Franz, Cerstin, et al. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>, vol. 8, no. 2, EMBO, 2007, pp. 165–72, doi:<a href=\"https://doi.org/10.1038/sj.embor.7400889\">10.1038/sj.embor.7400889</a>.","short":"C. Franz, R. Walczak, S. Yavuz, R. Santarella, M. Gentzel, P. Askjaer, V. Galy, M. Hetzer, I.W. Mattaj, W. Antonin, EMBO Reports 8 (2007) 165–172.","ista":"Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, Galy V, Hetzer M, Mattaj IW, Antonin W. 2007. MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO reports. 8(2), 165–172.","ama":"Franz C, Walczak R, Yavuz S, et al. MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO reports</i>. 2007;8(2):165-172. doi:<a href=\"https://doi.org/10.1038/sj.embor.7400889\">10.1038/sj.embor.7400889</a>","apa":"Franz, C., Walczak, R., Yavuz, S., Santarella, R., Gentzel, M., Askjaer, P., … Antonin, W. (2007). MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO Reports</i>. EMBO. <a href=\"https://doi.org/10.1038/sj.embor.7400889\">https://doi.org/10.1038/sj.embor.7400889</a>","ieee":"C. Franz <i>et al.</i>, “MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly,” <i>EMBO reports</i>, vol. 8, no. 2. EMBO, pp. 165–172, 2007.","chicago":"Franz, Cerstin, Rudolf Walczak, Sevil Yavuz, Rachel Santarella, Marc Gentzel, Peter Askjaer, Vincent Galy, Martin Hetzer, Iain W Mattaj, and Wolfram Antonin. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>. EMBO, 2007. <a href=\"https://doi.org/10.1038/sj.embor.7400889\">https://doi.org/10.1038/sj.embor.7400889</a>."},"date_updated":"2022-07-18T08:56:40Z","abstract":[{"text":"The metazoan nuclear envelope (NE) breaks down and re-forms during each cell cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport during interphase, assemble into the re-forming NE at the end of mitosis. Using in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal effect lethal), a recently discovered NE component in Caenorhabditis elegans, functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107–160 complex (Nup for nucleoporin), an important building block of the NPC, and is essential for the recruitment of the Nup107–160 complex to chromatin. We suggest that MEL-28 acts as a seeding point for NPC assembly.","lang":"eng"}],"day":"19","doi":"10.1038/sj.embor.7400889","extern":"1","volume":8}]