[{"pmid":1,"related_material":{"record":[{"id":"20149","status":"public","relation":"dissertation_contains"}]},"corr_author":"1","tmp":{"short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"article_processing_charge":"Yes (via OA deal)","publisher":"Springer Nature","volume":26,"author":[{"id":"26E95904-5160-11E9-9C0B-C5B0DC97E90F","first_name":"Patricia","orcid":"0000-0003-1681-508X","last_name":"Dos Reis Rodrigues","full_name":"Dos Reis Rodrigues, Patricia"},{"orcid":"0000-0001-6406-524X","first_name":"Mario","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E","full_name":"Avellaneda Sarrió, Mario","last_name":"Avellaneda Sarrió"},{"orcid":"0000-0002-8518-5926","first_name":"Nikola","id":"3795523E-F248-11E8-B48F-1D18A9856A87","last_name":"Canigova","full_name":"Canigova, Nikola"},{"id":"397A88EE-F248-11E8-B48F-1D18A9856A87","first_name":"Florian R","orcid":"0000-0001-6120-3723","full_name":"Gärtner, Florian R","last_name":"Gärtner"},{"first_name":"Kari","id":"368EE576-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7829-3518","last_name":"Vaahtomeri","full_name":"Vaahtomeri, Kari"},{"id":"3BE60946-F248-11E8-B48F-1D18A9856A87","first_name":"Michael","orcid":"0000-0003-4844-6311","last_name":"Riedl","full_name":"Riedl, Michael"},{"first_name":"Ingrid","id":"4C7D837E-F248-11E8-B48F-1D18A9856A87","last_name":"De Vries","full_name":"De Vries, Ingrid"},{"orcid":"0000-0001-5145-4609","id":"4515C308-F248-11E8-B48F-1D18A9856A87","first_name":"Jack","full_name":"Merrin, Jack","last_name":"Merrin"},{"full_name":"Hauschild, Robert","last_name":"Hauschild","first_name":"Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-9843-3522"},{"full_name":"Fukui, Yoshinori","last_name":"Fukui","first_name":"Yoshinori"},{"id":"40F05888-F248-11E8-B48F-1D18A9856A87","first_name":"Alba","orcid":"0000-0002-1009-9652","last_name":"Juanes Garcia","full_name":"Juanes Garcia, Alba"},{"orcid":"0000-0002-6620-9179","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","full_name":"Sixt, Michael K","last_name":"Sixt"}],"article_type":"letter_note","project":[{"name":"Pushing from within: Control of cell shape, integrity and motility by cytoskeletal pushing forces","_id":"bd91e723-d553-11ed-ba76-fe7eeb2185fd","grant_number":"101071793"},{"grant_number":"944-2020","_id":"c092d618-5a5b-11eb-8a69-f92e1e843fc8","name":"Bioelectric patrolling: the role of the local membrane potential in immune cell migration"}],"month":"08","department":[{"_id":"MiSi"},{"_id":"NanoFab"},{"_id":"Bio"}],"acknowledgement":"This research was supported by the Scientific Service Units of ISTA through resources provided by the Imaging and Optics, Preclinical and Lab Support Facilities. In particular, we thank M. A. Symth and F. G. G. Leite, from the Virus Service Team, who helped generating the lentiviral particles used in this study. We thank all the members of the Sixt group for valuable discussions and feedback, in particular, I. Mayer, for helping with T cell isolation and Z. (P.) Li for providing the Actin–GFP DC line. We are also thankful to J. Mandl and C. Shen for their feedback during the writing of this manuscript. This work was supported by a European Research Council grant ERC-SyG 101071793 to M.S. M.J.A. was supported by an HFSP Postdoctoral Fellowship LTF 177 2021 and A.J.G. by a Lise Meitner Fellowship of the FWF (Austrian Science Fund). Y.F. was supported by the AMED-CREST (JP19gm1310005), the Medical Research Center Initiative for High Depth Omics and CURE:JPMXP1323015486 for MIB, Kyushu University. Open access funding provided by Institute of Science and Technology (IST Austria).","doi":"10.1038/s41590-025-02211-w","oa":1,"title":"Migrating immune cells globally coordinate protrusive forces","date_created":"2025-07-27T22:01:26Z","oa_version":"Published Version","OA_type":"hybrid","publication_identifier":{"issn":["1529-2908"],"eissn":["1529-2916"]},"file":[{"access_level":"open_access","date_created":"2025-07-31T08:00:33Z","file_size":13514646,"content_type":"application/pdf","success":1,"file_name":"2025_NatureImmunology_ReisRodrigues.pdf","checksum":"0c725123dca7797c682609bff2c4c5ac","date_updated":"2025-07-31T08:00:33Z","file_id":"20096","relation":"main_file","creator":"dernst"}],"publication_status":"published","license":"https://creativecommons.org/licenses/by/4.0/","scopus_import":"1","PlanS_conform":"1","status":"public","page":"1258–1266","publication":"Nature Immunology","date_updated":"2026-04-07T12:36:25Z","acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"isi":1,"file_date_updated":"2025-07-31T08:00:33Z","date_published":"2025-08-01T00:00:00Z","OA_place":"publisher","intvolume":"        26","year":"2025","ddc":["570"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","has_accepted_license":"1","day":"01","citation":{"apa":"Dos Reis Rodrigues, P., Avellaneda Sarrió, M., Canigova, N., Gärtner, F. R., Vaahtomeri, K., Riedl, M., … Sixt, M. K. (2025). Migrating immune cells globally coordinate protrusive forces. <i>Nature Immunology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41590-025-02211-w\">https://doi.org/10.1038/s41590-025-02211-w</a>","mla":"Dos Reis Rodrigues, Patricia, et al. “Migrating Immune Cells Globally Coordinate Protrusive Forces.” <i>Nature Immunology</i>, vol. 26, Springer Nature, 2025, pp. 1258–1266, doi:<a href=\"https://doi.org/10.1038/s41590-025-02211-w\">10.1038/s41590-025-02211-w</a>.","short":"P. Dos Reis Rodrigues, M. Avellaneda Sarrió, N. Canigova, F.R. Gärtner, K. Vaahtomeri, M. Riedl, I. de Vries, J. Merrin, R. Hauschild, Y. Fukui, A. Juanes Garcia, M.K. Sixt, Nature Immunology 26 (2025) 1258–1266.","ieee":"P. Dos Reis Rodrigues <i>et al.</i>, “Migrating immune cells globally coordinate protrusive forces,” <i>Nature Immunology</i>, vol. 26. Springer Nature, pp. 1258–1266, 2025.","chicago":"Dos Reis Rodrigues, Patricia, Mario Avellaneda Sarrió, Nikola Canigova, Florian R Gärtner, Kari Vaahtomeri, Michael Riedl, Ingrid de Vries, et al. “Migrating Immune Cells Globally Coordinate Protrusive Forces.” <i>Nature Immunology</i>. Springer Nature, 2025. <a href=\"https://doi.org/10.1038/s41590-025-02211-w\">https://doi.org/10.1038/s41590-025-02211-w</a>.","ama":"Dos Reis Rodrigues P, Avellaneda Sarrió M, Canigova N, et al. Migrating immune cells globally coordinate protrusive forces. <i>Nature Immunology</i>. 2025;26:1258–1266. doi:<a href=\"https://doi.org/10.1038/s41590-025-02211-w\">10.1038/s41590-025-02211-w</a>","ista":"Dos Reis Rodrigues P, Avellaneda Sarrió M, Canigova N, Gärtner FR, Vaahtomeri K, Riedl M, de Vries I, Merrin J, Hauschild R, Fukui Y, Juanes Garcia A, Sixt MK. 2025. Migrating immune cells globally coordinate protrusive forces. Nature Immunology. 26, 1258–1266."},"language":[{"iso":"eng"}],"_id":"20082","abstract":[{"lang":"eng","text":"Efficient immune responses rely on the capacity of leukocytes to traverse diverse and complex tissues. To meet such changing environmental conditions, leukocytes usually adopt an ameboid configuration, using their forward-positioned nucleus as a probe to identify and follow the path of least resistance among pre-existing pores. We show that, in dense environments where even the largest pores preclude free passage, leukocytes position their nucleus behind the centrosome and organelles. The local compression imposed on the cell body by its surroundings triggers assembly of a central F-actin pool, located between cell front and nucleus. Central actin pushes outward to transiently dilate a path for organelles and nucleus. Pools of central and front actin are tightly coupled and experimental depletion of the central pool enhances actin accumulation and protrusion formation at the cell front. Although this shifted balance speeds up cells in permissive environments, migration in restrictive environments is impaired, as the unleashed leading edge dissociates from the trapped cell body. Our findings establish an actin regulatory loop that balances path dilation with advancement of the leading edge to maintain cellular coherence."}],"external_id":{"pmid":["40664976"],"isi":["001529134300001"]},"type":"journal_article","quality_controlled":"1"},{"date_published":"2024-07-18T00:00:00Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","year":"2024","intvolume":"        31","day":"18","citation":{"ista":"Avellaneda Sarrió M, Sixt MK. 2024. Rescuing T cells from stiff tumors. Cell Chemical Biology. 31(7), 1242–1243.","ama":"Avellaneda Sarrió M, Sixt MK. Rescuing T cells from stiff tumors. <i>Cell Chemical Biology</i>. 2024;31(7):1242-1243. doi:<a href=\"https://doi.org/10.1016/j.chembiol.2024.06.011\">10.1016/j.chembiol.2024.06.011</a>","chicago":"Avellaneda Sarrió, Mario, and Michael K Sixt. “Rescuing T Cells from Stiff Tumors.” <i>Cell Chemical Biology</i>. Elsevier, 2024. <a href=\"https://doi.org/10.1016/j.chembiol.2024.06.011\">https://doi.org/10.1016/j.chembiol.2024.06.011</a>.","ieee":"M. Avellaneda Sarrió and M. K. Sixt, “Rescuing T cells from stiff tumors,” <i>Cell Chemical Biology</i>, vol. 31, no. 7. Elsevier, pp. 1242–1243, 2024.","short":"M. Avellaneda Sarrió, M.K. Sixt, Cell Chemical Biology 31 (2024) 1242–1243.","mla":"Avellaneda Sarrió, Mario, and Michael K. Sixt. “Rescuing T Cells from Stiff Tumors.” <i>Cell Chemical Biology</i>, vol. 31, no. 7, Elsevier, 2024, pp. 1242–43, doi:<a href=\"https://doi.org/10.1016/j.chembiol.2024.06.011\">10.1016/j.chembiol.2024.06.011</a>.","apa":"Avellaneda Sarrió, M., &#38; Sixt, M. K. (2024). Rescuing T cells from stiff tumors. <i>Cell Chemical Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.chembiol.2024.06.011\">https://doi.org/10.1016/j.chembiol.2024.06.011</a>"},"quality_controlled":"1","type":"journal_article","external_id":{"isi":["001275725000001"],"pmid":["39029454"]},"_id":"17279","abstract":[{"lang":"eng","text":"In a recent issue of Cell, Zhang et al.1 demonstrate that mechanical features of a solid tumor can drive T cells into dysfunctionality and identify pathways that revert this “exhausted” state."}],"language":[{"iso":"eng"}],"scopus_import":"1","issue":"7","page":"1242-1243","status":"public","isi":1,"publication":"Cell Chemical Biology","date_updated":"2025-09-08T08:27:03Z","oa_version":"None","title":"Rescuing T cells from stiff tumors","date_created":"2024-07-21T22:01:00Z","publication_identifier":{"issn":["2451-9456"],"eissn":["2451-9448"]},"publication_status":"published","pmid":1,"publisher":"Elsevier","article_processing_charge":"No","corr_author":"1","department":[{"_id":"MiSi"}],"month":"07","article_type":"review","author":[{"first_name":"Mario","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E","orcid":"0000-0001-6406-524X","last_name":"Avellaneda Sarrió","full_name":"Avellaneda Sarrió, Mario"},{"last_name":"Sixt","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87"}],"volume":31,"doi":"10.1016/j.chembiol.2024.06.011"},{"status":"public","page":"278-318","publisher":"Royal Society of Chemistry","article_processing_charge":"No","editor":[{"first_name":"Sebastian","full_name":"Hiller, Sebastian","last_name":"Hiller"},{"last_name":"Liu","full_name":"Liu, Maili","first_name":"Maili"},{"full_name":"He, Lichun","last_name":"He","first_name":"Lichun"}],"doi":"10.1039/bk9781839165986-00278","month":"11","department":[{"_id":"MiSi"}],"author":[{"last_name":"Wruck","full_name":"Wruck, F.","first_name":"F."},{"last_name":"Avellaneda Sarrió","full_name":"Avellaneda Sarrió, Mario","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E","first_name":"Mario","orcid":"0000-0001-6406-524X"},{"full_name":"Naqvi, M. M.","last_name":"Naqvi","first_name":"M. M."},{"first_name":"E. J.","full_name":"Koers, E. J.","last_name":"Koers"},{"first_name":"K.","full_name":"Till, K.","last_name":"Till"},{"full_name":"Gross, L.","last_name":"Gross","first_name":"L."},{"full_name":"Moayed, F.","last_name":"Moayed","first_name":"F."},{"last_name":"Roland","full_name":"Roland, A.","first_name":"A."},{"first_name":"L. W. H. J.","last_name":"Heling","full_name":"Heling, L. W. H. J."},{"first_name":"A.","full_name":"Mashaghi, A.","last_name":"Mashaghi"},{"first_name":"S. J.","full_name":"Tans, S. J.","last_name":"Tans"}],"volume":29,"date_updated":"2024-01-23T12:01:53Z","publication":"Biophysics of Molecular Chaperones","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"isbn":["9781839162824"],"eisbn":["9781839165993"]},"year":"2023","intvolume":"        29","oa_version":"None","alternative_title":["New Developments in NMR"],"date_created":"2024-01-22T08:07:02Z","title":"Probing Single Chaperone Substrates","date_published":"2023-11-01T00:00:00Z","quality_controlled":"1","publication_status":"published","type":"book_chapter","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."}],"_id":"14848","language":[{"iso":"eng"}],"citation":{"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>","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.","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>.","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>.","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.","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.","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>"},"day":"01"},{"publication_status":"published","oa_version":"Preprint","title":"Weak catch bonds make strong networks","date_created":"2022-09-11T22:01:57Z","publication_identifier":{"issn":["1476-1122"],"eissn":["1476-4660"]},"article_type":"original","department":[{"_id":"MiSi"}],"month":"09","author":[{"first_name":"Yuval","last_name":"Mulla","full_name":"Mulla, Yuval"},{"full_name":"Avellaneda Sarrió, Mario","last_name":"Avellaneda Sarrió","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E","first_name":"Mario","orcid":"0000-0001-6406-524X"},{"first_name":"Antoine","last_name":"Roland","full_name":"Roland, Antoine"},{"first_name":"Lucia","last_name":"Baldauf","full_name":"Baldauf, Lucia"},{"full_name":"Jung, Wonyeong","last_name":"Jung","first_name":"Wonyeong"},{"last_name":"Kim","full_name":"Kim, Taeyoon","first_name":"Taeyoon"},{"full_name":"Tans, Sander J.","last_name":"Tans","first_name":"Sander J."},{"full_name":"Koenderink, Gijsje H.","last_name":"Koenderink","first_name":"Gijsje H."}],"volume":21,"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.).","doi":"10.1038/s41563-022-01288-0","oa":1,"pmid":1,"publisher":"Springer Nature","article_processing_charge":"No","day":"01","citation":{"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.","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.","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>.","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>.","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.","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>"},"type":"journal_article","quality_controlled":"1","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"}],"_id":"12085","language":[{"iso":"eng"}],"external_id":{"pmid":["36008604"],"isi":["000844592000002"]},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1101/2020.07.27.219618"}],"date_published":"2022-09-01T00:00:00Z","year":"2022","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","intvolume":"        21","isi":1,"publication":"Nature Materials","date_updated":"2023-08-03T14:08:47Z","scopus_import":"1","issue":"9","page":"1019-1023","status":"public"},{"date_published":"2022-03-01T00:00:00Z","intvolume":"         8","article_number":"eabl6293","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","ddc":["570"],"year":"2022","day":"01","citation":{"ista":"Naqvi MM, Avellaneda Sarrió M, Roth A, Koers EJ, Roland A, Sunderlikova V, Kramer G, Rye HS, Tans SJ. 2022. Protein chain collapse modulation and folding stimulation by GroEL-ES. Science Advances. 8(9), eabl6293.","ama":"Naqvi MM, Avellaneda Sarrió M, Roth A, et al. Protein chain collapse modulation and folding stimulation by GroEL-ES. <i>Science Advances</i>. 2022;8(9). doi:<a href=\"https://doi.org/10.1126/sciadv.abl6293\">10.1126/sciadv.abl6293</a>","chicago":"Naqvi, Mohsin M., Mario Avellaneda Sarrió, Andrew Roth, Eline J. Koers, Antoine Roland, Vanda Sunderlikova, Günter Kramer, Hays S. Rye, and Sander J. Tans. “Protein Chain Collapse Modulation and Folding Stimulation by GroEL-ES.” <i>Science Advances</i>. American Association for the Advancement of Science, 2022. <a href=\"https://doi.org/10.1126/sciadv.abl6293\">https://doi.org/10.1126/sciadv.abl6293</a>.","short":"M.M. Naqvi, M. Avellaneda Sarrió, A. Roth, E.J. Koers, A. Roland, V. Sunderlikova, G. Kramer, H.S. Rye, S.J. Tans, Science Advances 8 (2022).","ieee":"M. M. Naqvi <i>et al.</i>, “Protein chain collapse modulation and folding stimulation by GroEL-ES,” <i>Science Advances</i>, vol. 8, no. 9. American Association for the Advancement of Science, 2022.","mla":"Naqvi, Mohsin M., et al. “Protein Chain Collapse Modulation and Folding Stimulation by GroEL-ES.” <i>Science Advances</i>, vol. 8, no. 9, eabl6293, American Association for the Advancement of Science, 2022, doi:<a href=\"https://doi.org/10.1126/sciadv.abl6293\">10.1126/sciadv.abl6293</a>.","apa":"Naqvi, M. M., Avellaneda Sarrió, M., Roth, A., Koers, E. J., Roland, A., Sunderlikova, V., … Tans, S. J. (2022). Protein chain collapse modulation and folding stimulation by GroEL-ES. <i>Science Advances</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/sciadv.abl6293\">https://doi.org/10.1126/sciadv.abl6293</a>"},"has_accepted_license":"1","external_id":{"pmid":["35245117"]},"abstract":[{"lang":"eng","text":"The collapse of polypeptides is thought important to protein folding, aggregation, intrinsic disorder, and phase separation. However, whether polypeptide collapse is modulated in cells to control protein states is unclear. Here, using integrated protein manipulation and imaging, we show that the chaperonin GroEL-ES can accelerate the folding of proteins by strengthening their collapse. GroEL induces contractile forces in substrate chains, which draws them into the cavity and triggers a general compaction and discrete folding transitions, even for slow-folding proteins. This collapse enhancement is strongest in the nucleotide-bound states of GroEL and is aided by GroES binding to the cavity rim and by the amphiphilic C-terminal tails at the cavity bottom. Collapse modulation is distinct from other proposed GroEL-ES folding acceleration mechanisms, including steric confinement and misfold unfolding. Given the prevalence of collapse throughout the proteome, we conjecture that collapse modulation is more generally relevant within the protein quality control machinery."}],"_id":"17072","language":[{"iso":"eng"}],"quality_controlled":"1","type":"journal_article","issue":"9","scopus_import":"1","status":"public","publication":"Science Advances","date_updated":"2024-08-05T08:30:29Z","file_date_updated":"2024-07-31T12:01:51Z","title":"Protein chain collapse modulation and folding stimulation by GroEL-ES","date_created":"2024-05-29T06:12:19Z","oa_version":"Published Version","publication_identifier":{"issn":["2375-2548"]},"file":[{"access_level":"open_access","success":1,"content_type":"application/pdf","date_created":"2024-07-31T12:01:51Z","file_size":2404150,"checksum":"9511579306cce7e04107d3d6389ed614","file_name":"2022_ScienceAdv_Naqvi.pdf","creator":"dernst","date_updated":"2024-07-31T12:01:51Z","relation":"main_file","file_id":"17357"}],"publication_status":"published","pmid":1,"article_processing_charge":"Yes","tmp":{"short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"publisher":"American Association for the Advancement of Science","author":[{"first_name":"Mohsin M.","full_name":"Naqvi, Mohsin M.","last_name":"Naqvi"},{"full_name":"Avellaneda Sarrió, Mario","last_name":"Avellaneda Sarrió","orcid":"0000-0001-6406-524X","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E","first_name":"Mario"},{"first_name":"Andrew","last_name":"Roth","full_name":"Roth, Andrew"},{"first_name":"Eline J.","full_name":"Koers, Eline J.","last_name":"Koers"},{"first_name":"Antoine","last_name":"Roland","full_name":"Roland, Antoine"},{"first_name":"Vanda","last_name":"Sunderlikova","full_name":"Sunderlikova, Vanda"},{"full_name":"Kramer, Günter","last_name":"Kramer","first_name":"Günter"},{"first_name":"Hays S.","full_name":"Rye, Hays S.","last_name":"Rye"},{"first_name":"Sander J.","full_name":"Tans, Sander J.","last_name":"Tans"}],"volume":8,"month":"03","department":[{"_id":"MiSi"}],"article_type":"original","doi":"10.1126/sciadv.abl6293","oa":1,"acknowledgement":"We thank A. L. Horwich, K. Chakraborty, and B. Schuler for providing plasmids, and R. van Leeuwen, M. Mayer, J. van Zon, W. Noorduin, and P. R. ten Wolde for comments and critical reading of the manuscript. Work in the group of S.J.T. was supported by the Netherlands Organization for Scientific Research (NWO). Work in the group of H.S.R. was supported by a grant from the NIH (R01GM114405)."}]