[{"doi":"10.1039/bk9781839165986-00278","language":[{"iso":"eng"}],"year":"2023","publisher":"Royal Society of Chemistry","date_updated":"2024-01-23T12:01:53Z","status":"public","type":"book_chapter","author":[{"last_name":"Wruck","full_name":"Wruck, F.","first_name":"F."},{"full_name":"Avellaneda Sarrió, Mario","first_name":"Mario","orcid":"0000-0001-6406-524X","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E","last_name":"Avellaneda Sarrió"},{"full_name":"Naqvi, M. M.","first_name":"M. M.","last_name":"Naqvi"},{"last_name":"Koers","full_name":"Koers, E. J.","first_name":"E. J."},{"first_name":"K.","full_name":"Till, K.","last_name":"Till"},{"full_name":"Gross, L.","first_name":"L.","last_name":"Gross"},{"full_name":"Moayed, F.","first_name":"F.","last_name":"Moayed"},{"full_name":"Roland, A.","first_name":"A.","last_name":"Roland"},{"first_name":"L. W. H. J.","full_name":"Heling, L. W. H. J.","last_name":"Heling"},{"full_name":"Mashaghi, A.","first_name":"A.","last_name":"Mashaghi"},{"last_name":"Tans","first_name":"S. J.","full_name":"Tans, S. J."}],"_id":"14848","day":"01","publication_status":"published","oa_version":"None","page":"278-318","date_published":"2023-11-01T00:00:00Z","abstract":[{"lang":"eng","text":"Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function."}],"date_created":"2024-01-22T08:07:02Z","citation":{"short":"F. Wruck, M. Avellaneda Sarrió, M.M. Naqvi, E.J. Koers, K. Till, L. Gross, F. Moayed, A. Roland, L.W.H.J. Heling, A. Mashaghi, S.J. Tans, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 278–318.","ista":"Wruck F, Avellaneda Sarrió M, Naqvi MM, Koers EJ, Till K, Gross L, Moayed F, Roland A, Heling LWHJ, Mashaghi A, Tans SJ. 2023.Probing Single Chaperone Substrates. In: Biophysics of Molecular Chaperones. New Developments in NMR, vol. 29, 278–318.","apa":"Wruck, F., Avellaneda Sarrió, M., Naqvi, M. M., Koers, E. J., Till, K., Gross, L., … Tans, S. J. (2023). Probing Single Chaperone Substrates. In S. Hiller, M. Liu, &#38; L. He (Eds.), <i>Biophysics of Molecular Chaperones</i> (Vol. 29, pp. 278–318). Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/bk9781839165986-00278\">https://doi.org/10.1039/bk9781839165986-00278</a>","mla":"Wruck, F., et al. “Probing Single Chaperone Substrates.” <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023, pp. 278–318, doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00278\">10.1039/bk9781839165986-00278</a>.","ama":"Wruck F, Avellaneda Sarrió M, Naqvi MM, et al. Probing Single Chaperone Substrates. In: Hiller S, Liu M, He L, eds. <i>Biophysics of Molecular Chaperones</i>. Vol 29. Royal Society of Chemistry; 2023:278-318. doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00278\">10.1039/bk9781839165986-00278</a>","chicago":"Wruck, F., Mario Avellaneda Sarrió, M. M. Naqvi, E. J. Koers, K. Till, L. Gross, F. Moayed, et al. “Probing Single Chaperone Substrates.” In <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:278–318. Royal Society of Chemistry, 2023. <a href=\"https://doi.org/10.1039/bk9781839165986-00278\">https://doi.org/10.1039/bk9781839165986-00278</a>.","ieee":"F. Wruck <i>et al.</i>, “Probing Single Chaperone Substrates,” in <i>Biophysics of Molecular Chaperones</i>, vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023, pp. 278–318."},"department":[{"_id":"MiSi"}],"editor":[{"first_name":"Sebastian","full_name":"Hiller, Sebastian","last_name":"Hiller"},{"last_name":"Liu","full_name":"Liu, Maili","first_name":"Maili"},{"last_name":"He","first_name":"Lichun","full_name":"He, Lichun"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","intvolume":"        29","alternative_title":["New Developments in NMR"],"month":"11","publication_identifier":{"isbn":["9781839162824"],"eisbn":["9781839165993"]},"quality_controlled":"1","publication":"Biophysics of Molecular Chaperones","title":"Probing Single Chaperone Substrates","volume":29},{"issue":"9","scopus_import":"1","citation":{"ama":"Mulla Y, Avellaneda Sarrió M, Roland A, et al. Weak catch bonds make strong networks. <i>Nature Materials</i>. 2022;21(9):1019-1023. doi:<a href=\"https://doi.org/10.1038/s41563-022-01288-0\">10.1038/s41563-022-01288-0</a>","short":"Y. Mulla, M. Avellaneda Sarrió, A. Roland, L. Baldauf, W. Jung, T. Kim, S.J. Tans, G.H. Koenderink, Nature Materials 21 (2022) 1019–1023.","ista":"Mulla Y, Avellaneda Sarrió M, Roland A, Baldauf L, Jung W, Kim T, Tans SJ, Koenderink GH. 2022. Weak catch bonds make strong networks. Nature Materials. 21(9), 1019–1023.","mla":"Mulla, Yuval, et al. “Weak Catch Bonds Make Strong Networks.” <i>Nature Materials</i>, vol. 21, no. 9, Springer Nature, 2022, pp. 1019–23, doi:<a href=\"https://doi.org/10.1038/s41563-022-01288-0\">10.1038/s41563-022-01288-0</a>.","apa":"Mulla, Y., Avellaneda Sarrió, M., Roland, A., Baldauf, L., Jung, W., Kim, T., … Koenderink, G. H. (2022). Weak catch bonds make strong networks. <i>Nature Materials</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41563-022-01288-0\">https://doi.org/10.1038/s41563-022-01288-0</a>","ieee":"Y. Mulla <i>et al.</i>, “Weak catch bonds make strong networks,” <i>Nature Materials</i>, vol. 21, no. 9. Springer Nature, pp. 1019–1023, 2022.","chicago":"Mulla, Yuval, Mario Avellaneda Sarrió, Antoine Roland, Lucia Baldauf, Wonyeong Jung, Taeyoon Kim, Sander J. Tans, and Gijsje H. Koenderink. “Weak Catch Bonds Make Strong Networks.” <i>Nature Materials</i>. Springer Nature, 2022. <a href=\"https://doi.org/10.1038/s41563-022-01288-0\">https://doi.org/10.1038/s41563-022-01288-0</a>."},"publication":"Nature Materials","external_id":{"pmid":["36008604"],"isi":["000844592000002"]},"title":"Weak catch bonds make strong networks","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1101/2020.07.27.219618"}],"status":"public","date_updated":"2023-08-03T14:08:47Z","oa_version":"Preprint","page":"1019-1023","publication_status":"published","day":"01","abstract":[{"text":"Molecular catch bonds are ubiquitous in biology and essential for processes like leucocyte extravasion1 and cellular mechanosensing2. Unlike normal (slip) bonds, catch bonds strengthen under tension. The current paradigm is that this feature provides ‘strength on demand3’, thus enabling cells to increase rigidity under stress1,4,5,6. However, catch bonds are often weaker than slip bonds because they have cryptic binding sites that are usually buried7,8. Here we show that catch bonds render reconstituted cytoskeletal actin networks stronger than slip bonds, even though the individual bonds are weaker. Simulations show that slip bonds remain trapped in stress-free areas, whereas weak binding allows catch bonds to mitigate crack initiation by moving to high-tension areas. This ‘dissociation on demand’ explains how cells combine mechanical strength with the adaptability required for shape change, and is relevant to diseases where catch bonding is compromised7,9, including focal segmental glomerulosclerosis10 caused by the α-actinin-4 mutant studied here. We surmise that catch bonds are the key to create life-like materials.","lang":"eng"}],"article_processing_charge":"No","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","intvolume":"        21","date_created":"2022-09-11T22:01:57Z","pmid":1,"department":[{"_id":"MiSi"}],"acknowledgement":"We thank M. van Hecke and C. Alkemade for critical reading of the manuscript. We thank P. R. ten Wolde, K. Storm, W. Ellenbroek, C. Broedersz, D. Brueckner and M. Berger for fruitful discussions. We thank W. Brieher and V. Tang from the University of Illinois for the kind gift of purified α-actinin-4 (WT and the K255E point mutant) and their plasmids; M. Kuit-Vinkenoog and J. den Haan for actin and further purification of α-actinin-4; A. Goutou and I. Isturiz-Petitjean for co-sedimentation measurements and V. Sunderlíková for the design, mutagenesis, cloning and purifying of the α-actinin-4 constructs used in the single-molecule experiments. We gratefully acknowledge financial support from the following sources: research program of the Netherlands Organization for Scientific Research (NWO) (S.J.T., A.R. and M.J.A.); ERC Starting Grant (335672-MINICELL) (G.H.K. and Y.M.). ‘BaSyC—Building a Synthetic Cell’ Gravitation grant (024.003.019) of the Netherlands Ministry of Education, Culture and Science (OCW) and the Netherlands Organisation for Scientific Research (G.H.K. and L.B.); and support from the National Institutes of Health (1R01GM126256) (T.K. and W.J.).","isi":1,"article_type":"original","volume":21,"month":"09","quality_controlled":"1","publication_identifier":{"issn":["1476-1122"],"eissn":["1476-4660"]},"type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1038/s41563-022-01288-0","publisher":"Springer Nature","year":"2022","date_published":"2022-09-01T00:00:00Z","author":[{"last_name":"Mulla","full_name":"Mulla, Yuval","first_name":"Yuval"},{"first_name":"Mario","full_name":"Avellaneda Sarrió, Mario","orcid":"0000-0001-6406-524X","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E","last_name":"Avellaneda Sarrió"},{"first_name":"Antoine","full_name":"Roland, Antoine","last_name":"Roland"},{"first_name":"Lucia","full_name":"Baldauf, Lucia","last_name":"Baldauf"},{"full_name":"Jung, Wonyeong","first_name":"Wonyeong","last_name":"Jung"},{"full_name":"Kim, Taeyoon","first_name":"Taeyoon","last_name":"Kim"},{"last_name":"Tans","first_name":"Sander J.","full_name":"Tans, Sander J."},{"full_name":"Koenderink, Gijsje H.","first_name":"Gijsje H.","last_name":"Koenderink"}],"oa":1,"_id":"12085"}]