ID | 61868 |
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Author |
Mwangangi, Dennis M.
Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research)
Manser, Edward
Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research)
Robinson, Robert C.
Research Institute for Interdisciplinary Science (RIIS), Okayama University
ORCID
Kaken ID
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Abstract | Uncapping of actin filaments is essential for driving polymerization and depolymerization dynamics from capping protein–associated filaments; however, the mechanisms of uncapping leading to rapid disassembly are unknown. Here, we elucidated the x-ray crystal structure of the actin/twinfilin/capping protein complex to address the mechanisms of twinfilin uncapping of actin filaments. The twinfilin/capping protein complex binds to two G-actin subunits in an orientation that resembles the actin filament barbed end. This suggests an unanticipated mechanism by which twinfilin disrupts the stable capping of actin filaments by inducing a G-actin conformation in the two terminal actin subunits. Furthermore, twinfilin disorders critical actin-capping protein interactions, which will assist in the dissociation of capping protein, and may promote filament uncapping through a second mechanism involving V-1 competition for an actin-binding surface on capping protein. The extensive interactions with capping protein indicate that the evolutionary conserved role of twinfilin is to uncap actin filaments.
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Publication Title |
Science Advances
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Volume | volume7
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Issue | issue5
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Publisher | American Association for the Advancement of Science
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Start Page | eabd5271
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ISSN | 2375-2548
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Content Type |
Journal Article
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language |
English
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OAI-PMH Set |
岡山大学
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Copyright Holders | Copyright © 2021 The Authors
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File Version | publisher
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DOI | |
Related Url | isVersionOf https://doi.org/10.1126/sciadv.abd5271
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License | https://creativecommons.org/licenses/by-nc/4.0/
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