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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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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. |
format | Online Article Text |
id | pubmed-3842997 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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