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The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p

Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several eff...

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Autores principales: Grosshans, Bianka L., Andreeva, Anna, Gangar, Akanksha, Niessen, Sherry, Yates, John R., Brennwald, Patrick, Novick, Peter
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063532/
https://www.ncbi.nlm.nih.gov/pubmed/16390997
http://dx.doi.org/10.1083/jcb.200510016
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author Grosshans, Bianka L.
Andreeva, Anna
Gangar, Akanksha
Niessen, Sherry
Yates, John R.
Brennwald, Patrick
Novick, Peter
author_facet Grosshans, Bianka L.
Andreeva, Anna
Gangar, Akanksha
Niessen, Sherry
Yates, John R.
Brennwald, Patrick
Novick, Peter
author_sort Grosshans, Bianka L.
collection PubMed
description Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several effectors. Yet, only one Sec4p effector has been documented to date: the exocyst protein Sec15p. The exocyst is an octameric protein complex required for tethering secretory vesicles, which is a prerequisite for membrane fusion. In this study, we describe the identification of a second Sec4p effector, Sro7p, which is a member of the lethal giant larvae tumor suppressor family. Sec4-GTP binds to Sro7p in cell extracts as well as to purified Sro7p, and the two proteins can be coimmunoprecipitated. Furthermore, we demonstrate the formation of a ternary complex of Sec4-GTP, Sro7p, and the t-SNARE Sec9p. Genetic data support our conclusion that Sro7p functions downstream of Sec4p and further imply that Sro7p and the exocyst share partially overlapping functions, possibly in SNARE regulation.
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spelling pubmed-20635322008-03-19 The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p Grosshans, Bianka L. Andreeva, Anna Gangar, Akanksha Niessen, Sherry Yates, John R. Brennwald, Patrick Novick, Peter J Cell Biol Research Articles Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several effectors. Yet, only one Sec4p effector has been documented to date: the exocyst protein Sec15p. The exocyst is an octameric protein complex required for tethering secretory vesicles, which is a prerequisite for membrane fusion. In this study, we describe the identification of a second Sec4p effector, Sro7p, which is a member of the lethal giant larvae tumor suppressor family. Sec4-GTP binds to Sro7p in cell extracts as well as to purified Sro7p, and the two proteins can be coimmunoprecipitated. Furthermore, we demonstrate the formation of a ternary complex of Sec4-GTP, Sro7p, and the t-SNARE Sec9p. Genetic data support our conclusion that Sro7p functions downstream of Sec4p and further imply that Sro7p and the exocyst share partially overlapping functions, possibly in SNARE regulation. The Rockefeller University Press 2006-01-02 /pmc/articles/PMC2063532/ /pubmed/16390997 http://dx.doi.org/10.1083/jcb.200510016 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Grosshans, Bianka L.
Andreeva, Anna
Gangar, Akanksha
Niessen, Sherry
Yates, John R.
Brennwald, Patrick
Novick, Peter
The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p
title The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p
title_full The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p
title_fullStr The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p
title_full_unstemmed The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p
title_short The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p
title_sort yeast lgl family member sro7p is an effector of the secretory rab gtpase sec4p
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063532/
https://www.ncbi.nlm.nih.gov/pubmed/16390997
http://dx.doi.org/10.1083/jcb.200510016
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