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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...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2008
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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. |
format | Text |
id | pubmed-2213614 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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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