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Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia
Cofilin is a key regulator of the actin cytoskeleton. It can sever actin filaments, accelerate filament disassembly, act as a nucleation factor, recruit or antagonize other actin regulators, and control the pool of polymerization-competent actin monomers. In cells these actions have complex function...
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/PMC3708729/ https://www.ncbi.nlm.nih.gov/pubmed/23676663 http://dx.doi.org/10.1091/mbc.E13-03-0156 |
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author | Vitriol, Eric A. Wise, Ariel L. Berginski, Mathew E. Bamburg, James R. Zheng, James Q. |
author_facet | Vitriol, Eric A. Wise, Ariel L. Berginski, Mathew E. Bamburg, James R. Zheng, James Q. |
author_sort | Vitriol, Eric A. |
collection | PubMed |
description | Cofilin is a key regulator of the actin cytoskeleton. It can sever actin filaments, accelerate filament disassembly, act as a nucleation factor, recruit or antagonize other actin regulators, and control the pool of polymerization-competent actin monomers. In cells these actions have complex functional outputs. The timing and localization of cofilin activity are carefully regulated, and thus global, long-term perturbations may not be sufficient to probe its precise function. To better understand cofilin's spatiotemporal action in cells, we implemented chromophore-assisted laser inactivation (CALI) to instantly and specifically inactivate it. In addition to globally inhibiting actin turnover, CALI of cofilin generated several profound effects on the lamellipodia, including an increase of F-actin, a rearward expansion of the actin network, and a reduction in retrograde flow speed. These results support the hypothesis that the principal role of cofilin in lamellipodia at steady state is to break down F-actin, control filament turnover, and regulate the rate of retrograde flow. |
format | Online Article Text |
id | pubmed-3708729 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-37087292013-09-30 Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia Vitriol, Eric A. Wise, Ariel L. Berginski, Mathew E. Bamburg, James R. Zheng, James Q. Mol Biol Cell Articles Cofilin is a key regulator of the actin cytoskeleton. It can sever actin filaments, accelerate filament disassembly, act as a nucleation factor, recruit or antagonize other actin regulators, and control the pool of polymerization-competent actin monomers. In cells these actions have complex functional outputs. The timing and localization of cofilin activity are carefully regulated, and thus global, long-term perturbations may not be sufficient to probe its precise function. To better understand cofilin's spatiotemporal action in cells, we implemented chromophore-assisted laser inactivation (CALI) to instantly and specifically inactivate it. In addition to globally inhibiting actin turnover, CALI of cofilin generated several profound effects on the lamellipodia, including an increase of F-actin, a rearward expansion of the actin network, and a reduction in retrograde flow speed. These results support the hypothesis that the principal role of cofilin in lamellipodia at steady state is to break down F-actin, control filament turnover, and regulate the rate of retrograde flow. The American Society for Cell Biology 2013-07-15 /pmc/articles/PMC3708729/ /pubmed/23676663 http://dx.doi.org/10.1091/mbc.E13-03-0156 Text en © 2013 Vitriol 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 Vitriol, Eric A. Wise, Ariel L. Berginski, Mathew E. Bamburg, James R. Zheng, James Q. Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia |
title | Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia |
title_full | Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia |
title_fullStr | Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia |
title_full_unstemmed | Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia |
title_short | Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia |
title_sort | instantaneous inactivation of cofilin reveals its function of f-actin disassembly in lamellipodia |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3708729/ https://www.ncbi.nlm.nih.gov/pubmed/23676663 http://dx.doi.org/10.1091/mbc.E13-03-0156 |
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