Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Russo, Ashley J., Mathiowetz, Alyssa J., Hong, Steven, Welch, Matthew D., Campellone, Kenneth G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2016
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
_version_ 1782421044771946496
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
work_keys_str_mv AT russoashleyj rab1recruitswhammduringmembraneremodelingbutlimitsactinnucleation
AT mathiowetzalyssaj rab1recruitswhammduringmembraneremodelingbutlimitsactinnucleation
AT hongsteven rab1recruitswhammduringmembraneremodelingbutlimitsactinnucleation
AT welchmatthewd rab1recruitswhammduringmembraneremodelingbutlimitsactinnucleation
AT campellonekennethg rab1recruitswhammduringmembraneremodelingbutlimitsactinnucleation