Cargando…

Identification and characterization of multiple novel Rab–myosin Va interactions

Myosin Va is a widely expressed actin-based motor protein that binds members of the Rab GTPase family (3A, 8A, 10, 11A, 27A) and is implicated in many intracellular trafficking processes. To our knowledge, myosin Va has not been tested in a systematic screen for interactions with the entire Rab GTPa...

Descripción completa

Detalles Bibliográficos
Autores principales: Lindsay, Andrew J., Jollivet, Florence, Horgan, Conor P., Khan, Amir R., Raposo, Graça, McCaffrey, Mary W., Goud, Bruno
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814135/
https://www.ncbi.nlm.nih.gov/pubmed/24006491
http://dx.doi.org/10.1091/mbc.E13-05-0236
_version_ 1782289211739602944
author Lindsay, Andrew J.
Jollivet, Florence
Horgan, Conor P.
Khan, Amir R.
Raposo, Graça
McCaffrey, Mary W.
Goud, Bruno
author_facet Lindsay, Andrew J.
Jollivet, Florence
Horgan, Conor P.
Khan, Amir R.
Raposo, Graça
McCaffrey, Mary W.
Goud, Bruno
author_sort Lindsay, Andrew J.
collection PubMed
description Myosin Va is a widely expressed actin-based motor protein that binds members of the Rab GTPase family (3A, 8A, 10, 11A, 27A) and is implicated in many intracellular trafficking processes. To our knowledge, myosin Va has not been tested in a systematic screen for interactions with the entire Rab GTPase family. To that end, we report a yeast two-hybrid screen of all human Rabs for myosin Va-binding ability and reveal 10 novel interactions (3B, 3C, 3D, 6A, 6A′, 6B, 11B, 14, 25, 39B), which include interactions with three new Rab subfamilies (Rab6, Rab14, Rab39B). Of interest, myosin Va interacts with only a subset of the Rabs associated with the endocytic recycling and post-Golgi secretory systems. We demonstrate that myosin Va has three distinct Rab-binding domains on disparate regions of the motor (central stalk, an alternatively spliced exon, and the globular tail). Although the total pool of myosin Va is shared by several Rabs, Rab10 and Rab11 appear to be the major determinants of its recruitment to intracellular membranes. We also present evidence that myosin Va is necessary for maintaining a peripheral distribution of Rab11- and Rab14-positive endosomes.
format Online
Article
Text
id pubmed-3814135
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher The American Society for Cell Biology
record_format MEDLINE/PubMed
spelling pubmed-38141352014-01-16 Identification and characterization of multiple novel Rab–myosin Va interactions Lindsay, Andrew J. Jollivet, Florence Horgan, Conor P. Khan, Amir R. Raposo, Graça McCaffrey, Mary W. Goud, Bruno Mol Biol Cell Articles Myosin Va is a widely expressed actin-based motor protein that binds members of the Rab GTPase family (3A, 8A, 10, 11A, 27A) and is implicated in many intracellular trafficking processes. To our knowledge, myosin Va has not been tested in a systematic screen for interactions with the entire Rab GTPase family. To that end, we report a yeast two-hybrid screen of all human Rabs for myosin Va-binding ability and reveal 10 novel interactions (3B, 3C, 3D, 6A, 6A′, 6B, 11B, 14, 25, 39B), which include interactions with three new Rab subfamilies (Rab6, Rab14, Rab39B). Of interest, myosin Va interacts with only a subset of the Rabs associated with the endocytic recycling and post-Golgi secretory systems. We demonstrate that myosin Va has three distinct Rab-binding domains on disparate regions of the motor (central stalk, an alternatively spliced exon, and the globular tail). Although the total pool of myosin Va is shared by several Rabs, Rab10 and Rab11 appear to be the major determinants of its recruitment to intracellular membranes. We also present evidence that myosin Va is necessary for maintaining a peripheral distribution of Rab11- and Rab14-positive endosomes. The American Society for Cell Biology 2013-11-01 /pmc/articles/PMC3814135/ /pubmed/24006491 http://dx.doi.org/10.1091/mbc.E13-05-0236 Text en © 2013 Lindsay 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
Lindsay, Andrew J.
Jollivet, Florence
Horgan, Conor P.
Khan, Amir R.
Raposo, Graça
McCaffrey, Mary W.
Goud, Bruno
Identification and characterization of multiple novel Rab–myosin Va interactions
title Identification and characterization of multiple novel Rab–myosin Va interactions
title_full Identification and characterization of multiple novel Rab–myosin Va interactions
title_fullStr Identification and characterization of multiple novel Rab–myosin Va interactions
title_full_unstemmed Identification and characterization of multiple novel Rab–myosin Va interactions
title_short Identification and characterization of multiple novel Rab–myosin Va interactions
title_sort identification and characterization of multiple novel rab–myosin va interactions
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814135/
https://www.ncbi.nlm.nih.gov/pubmed/24006491
http://dx.doi.org/10.1091/mbc.E13-05-0236
work_keys_str_mv AT lindsayandrewj identificationandcharacterizationofmultiplenovelrabmyosinvainteractions
AT jollivetflorence identificationandcharacterizationofmultiplenovelrabmyosinvainteractions
AT horganconorp identificationandcharacterizationofmultiplenovelrabmyosinvainteractions
AT khanamirr identificationandcharacterizationofmultiplenovelrabmyosinvainteractions
AT raposograca identificationandcharacterizationofmultiplenovelrabmyosinvainteractions
AT mccaffreymaryw identificationandcharacterizationofmultiplenovelrabmyosinvainteractions
AT goudbruno identificationandcharacterizationofmultiplenovelrabmyosinvainteractions