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αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors

The actin-binding protein αE-catenin may contribute to transitions between cell migration and cell–cell adhesion that depend on remodeling the actin cytoskeleton, but the underlying mechanisms are unknown. We show that the αE-catenin actin-binding domain (ABD) binds cooperatively to individual actin...

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Autores principales: Hansen, Scott D., Kwiatkowski, Adam V., Ouyang, Chung-Yueh, Liu, HongJun, Pokutta, Sabine, Watkins, Simon C., Volkmann, Niels, Hanein, Dorit, Weis, William I., Mullins, R. Dyche, Nelson, W. James
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3842997/
https://www.ncbi.nlm.nih.gov/pubmed/24068324
http://dx.doi.org/10.1091/mbc.E13-07-0388
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author Hansen, Scott D.
Kwiatkowski, Adam V.
Ouyang, Chung-Yueh
Liu, HongJun
Pokutta, Sabine
Watkins, Simon C.
Volkmann, Niels
Hanein, Dorit
Weis, William I.
Mullins, R. Dyche
Nelson, W. James
author_facet Hansen, Scott D.
Kwiatkowski, Adam V.
Ouyang, Chung-Yueh
Liu, HongJun
Pokutta, Sabine
Watkins, Simon C.
Volkmann, Niels
Hanein, Dorit
Weis, William I.
Mullins, R. Dyche
Nelson, W. James
author_sort Hansen, Scott D.
collection PubMed
description The actin-binding protein αE-catenin may contribute to transitions between cell migration and cell–cell adhesion that depend on remodeling the actin cytoskeleton, but the underlying mechanisms are unknown. We show that the αE-catenin actin-binding domain (ABD) binds cooperatively to individual actin filaments and that binding is accompanied by a conformational change in the actin protomer that affects filament structure. αE-catenin ABD binding limits barbed-end growth, especially in actin filament bundles. αE-catenin ABD inhibits actin filament branching by the Arp2/3 complex and severing by cofilin, both of which contact regions of the actin protomer that are structurally altered by αE-catenin ABD binding. In epithelial cells, there is little correlation between the distribution of αE-catenin and the Arp2/3 complex at developing cell–cell contacts. Our results indicate that αE-catenin binding to filamentous actin favors assembly of unbranched filament bundles that are protected from severing over more dynamic, branched filament arrays.
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spelling pubmed-38429972014-02-16 αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors Hansen, Scott D. Kwiatkowski, Adam V. Ouyang, Chung-Yueh Liu, HongJun Pokutta, Sabine Watkins, Simon C. Volkmann, Niels Hanein, Dorit Weis, William I. Mullins, R. Dyche Nelson, W. James Mol Biol Cell Articles The actin-binding protein αE-catenin may contribute to transitions between cell migration and cell–cell adhesion that depend on remodeling the actin cytoskeleton, but the underlying mechanisms are unknown. We show that the αE-catenin actin-binding domain (ABD) binds cooperatively to individual actin filaments and that binding is accompanied by a conformational change in the actin protomer that affects filament structure. αE-catenin ABD binding limits barbed-end growth, especially in actin filament bundles. αE-catenin ABD inhibits actin filament branching by the Arp2/3 complex and severing by cofilin, both of which contact regions of the actin protomer that are structurally altered by αE-catenin ABD binding. In epithelial cells, there is little correlation between the distribution of αE-catenin and the Arp2/3 complex at developing cell–cell contacts. Our results indicate that αE-catenin binding to filamentous actin favors assembly of unbranched filament bundles that are protected from severing over more dynamic, branched filament arrays. The American Society for Cell Biology 2013-12-01 /pmc/articles/PMC3842997/ /pubmed/24068324 http://dx.doi.org/10.1091/mbc.E13-07-0388 Text en © 2013 Hansen et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Hansen, Scott D.
Kwiatkowski, Adam V.
Ouyang, Chung-Yueh
Liu, HongJun
Pokutta, Sabine
Watkins, Simon C.
Volkmann, Niels
Hanein, Dorit
Weis, William I.
Mullins, R. Dyche
Nelson, W. James
αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
title αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
title_full αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
title_fullStr αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
title_full_unstemmed αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
title_short αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
title_sort αe-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3842997/
https://www.ncbi.nlm.nih.gov/pubmed/24068324
http://dx.doi.org/10.1091/mbc.E13-07-0388
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