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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...
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/PMC3814135/ https://www.ncbi.nlm.nih.gov/pubmed/24006491 http://dx.doi.org/10.1091/mbc.E13-05-0236 |
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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 |
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