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Physiological role of the interaction between CARMIL1 and capping protein
The regulation of free barbed ends is central to the control of dynamic actin assembly and actin-based motility in cells. Capping protein (CP) is known to regulate barbed ends and control actin assembly in cells. The CARMIL family of proteins can bind and inhibit CP in vitro, but the physiological s...
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/PMC3784379/ https://www.ncbi.nlm.nih.gov/pubmed/23904264 http://dx.doi.org/10.1091/mbc.E13-05-0270 |
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author | Edwards, Marc Liang, Yun Kim, Taekyung Cooper, John A. |
author_facet | Edwards, Marc Liang, Yun Kim, Taekyung Cooper, John A. |
author_sort | Edwards, Marc |
collection | PubMed |
description | The regulation of free barbed ends is central to the control of dynamic actin assembly and actin-based motility in cells. Capping protein (CP) is known to regulate barbed ends and control actin assembly in cells. The CARMIL family of proteins can bind and inhibit CP in vitro, but the physiological significance of the interaction of CARMIL with CP in cells is poorly understood. Mammalian cells lacking CARMIL1 have defects in lamellipodia, macropinocytosis, cell migration, and Rac1 activation. Here we investigate the physiological significance of the CARMIL1–CP interaction, using a point mutant with a well-defined biochemical defect. We find that the CARMIL1–CP interaction is essential for the assembly of lamellipodia, the formation of ruffles, and the process of macropinocytosis. In contrast, the interaction of CARMIL1 with CP shows little to no importance for other functions of CARMIL1, including localization of CARMIL1 to the membrane, activation of Rac1, and cell migration. One implication is that lamellipodia are only marginally important for cell migration in a wound-healing model. The results also suggest that the ability of CARMIL1 to inhibit CP in cells may be regulated. |
format | Online Article Text |
id | pubmed-3784379 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-37843792013-12-16 Physiological role of the interaction between CARMIL1 and capping protein Edwards, Marc Liang, Yun Kim, Taekyung Cooper, John A. Mol Biol Cell Articles The regulation of free barbed ends is central to the control of dynamic actin assembly and actin-based motility in cells. Capping protein (CP) is known to regulate barbed ends and control actin assembly in cells. The CARMIL family of proteins can bind and inhibit CP in vitro, but the physiological significance of the interaction of CARMIL with CP in cells is poorly understood. Mammalian cells lacking CARMIL1 have defects in lamellipodia, macropinocytosis, cell migration, and Rac1 activation. Here we investigate the physiological significance of the CARMIL1–CP interaction, using a point mutant with a well-defined biochemical defect. We find that the CARMIL1–CP interaction is essential for the assembly of lamellipodia, the formation of ruffles, and the process of macropinocytosis. In contrast, the interaction of CARMIL1 with CP shows little to no importance for other functions of CARMIL1, including localization of CARMIL1 to the membrane, activation of Rac1, and cell migration. One implication is that lamellipodia are only marginally important for cell migration in a wound-healing model. The results also suggest that the ability of CARMIL1 to inhibit CP in cells may be regulated. The American Society for Cell Biology 2013-10-01 /pmc/articles/PMC3784379/ /pubmed/23904264 http://dx.doi.org/10.1091/mbc.E13-05-0270 Text en © 2013 Edwards 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 Edwards, Marc Liang, Yun Kim, Taekyung Cooper, John A. Physiological role of the interaction between CARMIL1 and capping protein |
title | Physiological role of the interaction between CARMIL1 and capping protein |
title_full | Physiological role of the interaction between CARMIL1 and capping protein |
title_fullStr | Physiological role of the interaction between CARMIL1 and capping protein |
title_full_unstemmed | Physiological role of the interaction between CARMIL1 and capping protein |
title_short | Physiological role of the interaction between CARMIL1 and capping protein |
title_sort | physiological role of the interaction between carmil1 and capping protein |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3784379/ https://www.ncbi.nlm.nih.gov/pubmed/23904264 http://dx.doi.org/10.1091/mbc.E13-05-0270 |
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