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Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation
Small G-proteins are key regulatory molecules that activate the actin nucleation machinery to drive cytoskeletal rearrangements during plasma membrane remodeling. However, the ability of small G-proteins to interact with nucleation factors on internal membranes to control trafficking processes has n...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4791140/ https://www.ncbi.nlm.nih.gov/pubmed/26823012 http://dx.doi.org/10.1091/mbc.E15-07-0508 |
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author | Russo, Ashley J. Mathiowetz, Alyssa J. Hong, Steven Welch, Matthew D. Campellone, Kenneth G. |
author_facet | Russo, Ashley J. Mathiowetz, Alyssa J. Hong, Steven Welch, Matthew D. Campellone, Kenneth G. |
author_sort | Russo, Ashley J. |
collection | PubMed |
description | Small G-proteins are key regulatory molecules that activate the actin nucleation machinery to drive cytoskeletal rearrangements during plasma membrane remodeling. However, the ability of small G-proteins to interact with nucleation factors on internal membranes to control trafficking processes has not been well characterized. Here we investigated roles for members of the Rho, Arf, and Rab G-protein families in regulating WASP homologue associated with actin, membranes, and microtubules (WHAMM), an activator of Arp2/3 complex–mediated actin nucleation. We found that Rab1 stimulated the formation and elongation of WHAMM-associated membrane tubules in cells. Active Rab1 recruited WHAMM to dynamic tubulovesicular structures in fibroblasts, and an active prenylated version of Rab1 bound directly to an N-terminal domain of WHAMM in vitro. In contrast to other G-protein–nucleation factor interactions, Rab1 binding inhibited WHAMM-mediated actin assembly. This ability of Rab1 to regulate WHAMM and the Arp2/3 complex represents a distinct strategy for membrane remodeling in which a Rab G-protein recruits the actin nucleation machinery but dampens its activity. |
format | Online Article Text |
id | pubmed-4791140 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-47911402016-05-30 Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation Russo, Ashley J. Mathiowetz, Alyssa J. Hong, Steven Welch, Matthew D. Campellone, Kenneth G. Mol Biol Cell Articles Small G-proteins are key regulatory molecules that activate the actin nucleation machinery to drive cytoskeletal rearrangements during plasma membrane remodeling. However, the ability of small G-proteins to interact with nucleation factors on internal membranes to control trafficking processes has not been well characterized. Here we investigated roles for members of the Rho, Arf, and Rab G-protein families in regulating WASP homologue associated with actin, membranes, and microtubules (WHAMM), an activator of Arp2/3 complex–mediated actin nucleation. We found that Rab1 stimulated the formation and elongation of WHAMM-associated membrane tubules in cells. Active Rab1 recruited WHAMM to dynamic tubulovesicular structures in fibroblasts, and an active prenylated version of Rab1 bound directly to an N-terminal domain of WHAMM in vitro. In contrast to other G-protein–nucleation factor interactions, Rab1 binding inhibited WHAMM-mediated actin assembly. This ability of Rab1 to regulate WHAMM and the Arp2/3 complex represents a distinct strategy for membrane remodeling in which a Rab G-protein recruits the actin nucleation machinery but dampens its activity. The American Society for Cell Biology 2016-03-15 /pmc/articles/PMC4791140/ /pubmed/26823012 http://dx.doi.org/10.1091/mbc.E15-07-0508 Text en © 2016 Russo 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 for Cell Biology. |
spellingShingle | Articles Russo, Ashley J. Mathiowetz, Alyssa J. Hong, Steven Welch, Matthew D. Campellone, Kenneth G. Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation |
title | Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation |
title_full | Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation |
title_fullStr | Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation |
title_full_unstemmed | Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation |
title_short | Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation |
title_sort | rab1 recruits whamm during membrane remodeling but limits actin nucleation |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4791140/ https://www.ncbi.nlm.nih.gov/pubmed/26823012 http://dx.doi.org/10.1091/mbc.E15-07-0508 |
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