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Membrane association and functional regulation of Sec3 by phospholipids and Cdc42

The exocyst is an octameric protein complex implicated in tethering post-Golgi secretory vesicles at the plasma membrane in preparation for fusion. However, it is not clear how the exocyst is targeted to and physically associates with specific domains of the plasma membrane and how its functions are...

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Autores principales: Zhang, Xiaoyu, Orlando, Kelly, He, Bing, Xi, Fengong, Zhang, Jian, Zajac, Allison, Guo, Wei
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213614/
https://www.ncbi.nlm.nih.gov/pubmed/18195105
http://dx.doi.org/10.1083/jcb.200704128
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author Zhang, Xiaoyu
Orlando, Kelly
He, Bing
Xi, Fengong
Zhang, Jian
Zajac, Allison
Guo, Wei
author_facet Zhang, Xiaoyu
Orlando, Kelly
He, Bing
Xi, Fengong
Zhang, Jian
Zajac, Allison
Guo, Wei
author_sort Zhang, Xiaoyu
collection PubMed
description The exocyst is an octameric protein complex implicated in tethering post-Golgi secretory vesicles at the plasma membrane in preparation for fusion. However, it is not clear how the exocyst is targeted to and physically associates with specific domains of the plasma membrane and how its functions are regulated at those regions. We demonstrate that the N terminus of the exocyst component Sec3 directly interacts with phosphatidylinositol 4,5-bisphosphate. In addition, we have identified key residues in Sec3 that are critical for its binding to the guanosine triphosphate–bound form of Cdc42. Genetic analyses indicate that the dual interactions of Sec3 with phospholipids and Cdc42 control its function in yeast cells. Disrupting these interactions not only blocks exocytosis and affects exocyst polarization but also leads to defects in cell morphogenesis. We propose that the interactions of Sec3 with phospholipids and Cdc42 play important roles in exocytosis and polarized cell growth.
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spelling pubmed-22136142008-07-14 Membrane association and functional regulation of Sec3 by phospholipids and Cdc42 Zhang, Xiaoyu Orlando, Kelly He, Bing Xi, Fengong Zhang, Jian Zajac, Allison Guo, Wei J Cell Biol Research Articles The exocyst is an octameric protein complex implicated in tethering post-Golgi secretory vesicles at the plasma membrane in preparation for fusion. However, it is not clear how the exocyst is targeted to and physically associates with specific domains of the plasma membrane and how its functions are regulated at those regions. We demonstrate that the N terminus of the exocyst component Sec3 directly interacts with phosphatidylinositol 4,5-bisphosphate. In addition, we have identified key residues in Sec3 that are critical for its binding to the guanosine triphosphate–bound form of Cdc42. Genetic analyses indicate that the dual interactions of Sec3 with phospholipids and Cdc42 control its function in yeast cells. Disrupting these interactions not only blocks exocytosis and affects exocyst polarization but also leads to defects in cell morphogenesis. We propose that the interactions of Sec3 with phospholipids and Cdc42 play important roles in exocytosis and polarized cell growth. The Rockefeller University Press 2008-01-14 /pmc/articles/PMC2213614/ /pubmed/18195105 http://dx.doi.org/10.1083/jcb.200704128 Text en Copyright © 2008, The Rockefeller University Press 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
Zhang, Xiaoyu
Orlando, Kelly
He, Bing
Xi, Fengong
Zhang, Jian
Zajac, Allison
Guo, Wei
Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
title Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
title_full Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
title_fullStr Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
title_full_unstemmed Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
title_short Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
title_sort membrane association and functional regulation of sec3 by phospholipids and cdc42
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213614/
https://www.ncbi.nlm.nih.gov/pubmed/18195105
http://dx.doi.org/10.1083/jcb.200704128
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