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Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators
Reinforcement of actin stress fibers in response to mechanical stimulation depends on a posttranslational mechanism that requires the LIM protein zyxin. The C-terminal LIM region of zyxin directs the force-sensitive accumulation of zyxin on actin stress fibers. The N-terminal region of zyxin promote...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3350550/ https://www.ncbi.nlm.nih.gov/pubmed/22456508 http://dx.doi.org/10.1091/mbc.E11-12-1057 |
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author | Hoffman, Laura M. Jensen, Christopher C. Chaturvedi, Aashi Yoshigi, Masaaki Beckerle, Mary C. |
author_facet | Hoffman, Laura M. Jensen, Christopher C. Chaturvedi, Aashi Yoshigi, Masaaki Beckerle, Mary C. |
author_sort | Hoffman, Laura M. |
collection | PubMed |
description | Reinforcement of actin stress fibers in response to mechanical stimulation depends on a posttranslational mechanism that requires the LIM protein zyxin. The C-terminal LIM region of zyxin directs the force-sensitive accumulation of zyxin on actin stress fibers. The N-terminal region of zyxin promotes actin reinforcement even when Rho kinase is inhibited. The mechanosensitive integrin effector p130Cas binds zyxin but is not required for mitogen-activated protein kinase–dependent zyxin phosphorylation or stress fiber remodeling in cells exposed to uniaxial cyclic stretch. α-Actinin and Ena/VASP proteins bind to the stress fiber reinforcement domain of zyxin. Mutation of their docking sites reveals that zyxin is required for recruitment of both groups of proteins to regions of stress fiber remodeling. Zyxin-null cells reconstituted with zyxin variants that lack either α-actinin or Ena/VASP-binding capacity display compromised response to mechanical stimulation. Our findings define a bipartite mechanism for stretch-induced actin remodeling that involves mechanosensitive targeting of zyxin to actin stress fibers and localized recruitment of actin regulatory machinery. |
format | Online Article Text |
id | pubmed-3350550 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33505502012-07-30 Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators Hoffman, Laura M. Jensen, Christopher C. Chaturvedi, Aashi Yoshigi, Masaaki Beckerle, Mary C. Mol Biol Cell Articles Reinforcement of actin stress fibers in response to mechanical stimulation depends on a posttranslational mechanism that requires the LIM protein zyxin. The C-terminal LIM region of zyxin directs the force-sensitive accumulation of zyxin on actin stress fibers. The N-terminal region of zyxin promotes actin reinforcement even when Rho kinase is inhibited. The mechanosensitive integrin effector p130Cas binds zyxin but is not required for mitogen-activated protein kinase–dependent zyxin phosphorylation or stress fiber remodeling in cells exposed to uniaxial cyclic stretch. α-Actinin and Ena/VASP proteins bind to the stress fiber reinforcement domain of zyxin. Mutation of their docking sites reveals that zyxin is required for recruitment of both groups of proteins to regions of stress fiber remodeling. Zyxin-null cells reconstituted with zyxin variants that lack either α-actinin or Ena/VASP-binding capacity display compromised response to mechanical stimulation. Our findings define a bipartite mechanism for stretch-induced actin remodeling that involves mechanosensitive targeting of zyxin to actin stress fibers and localized recruitment of actin regulatory machinery. The American Society for Cell Biology 2012-05-15 /pmc/articles/PMC3350550/ /pubmed/22456508 http://dx.doi.org/10.1091/mbc.E11-12-1057 Text en © 2012 Hoffman 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 Hoffman, Laura M. Jensen, Christopher C. Chaturvedi, Aashi Yoshigi, Masaaki Beckerle, Mary C. Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators |
title | Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators |
title_full | Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators |
title_fullStr | Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators |
title_full_unstemmed | Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators |
title_short | Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators |
title_sort | stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3350550/ https://www.ncbi.nlm.nih.gov/pubmed/22456508 http://dx.doi.org/10.1091/mbc.E11-12-1057 |
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