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Plasma membrane microdomains regulate turnover of transport proteins in yeast
In this study, we investigate whether the stable segregation of proteins and lipids within the yeast plasma membrane serves a particular biological function. We show that 21 proteins cluster within or associate with the ergosterol-rich membrane compartment of Can1 (MCC). However, proteins of the end...
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/PMC2600745/ https://www.ncbi.nlm.nih.gov/pubmed/19064668 http://dx.doi.org/10.1083/jcb.200806035 |
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author | Grossmann, Guido Malinsky, Jan Stahlschmidt, Wiebke Loibl, Martin Weig-Meckl, Ina Frommer, Wolf B. Opekarová, Miroslava Tanner, Widmar |
author_facet | Grossmann, Guido Malinsky, Jan Stahlschmidt, Wiebke Loibl, Martin Weig-Meckl, Ina Frommer, Wolf B. Opekarová, Miroslava Tanner, Widmar |
author_sort | Grossmann, Guido |
collection | PubMed |
description | In this study, we investigate whether the stable segregation of proteins and lipids within the yeast plasma membrane serves a particular biological function. We show that 21 proteins cluster within or associate with the ergosterol-rich membrane compartment of Can1 (MCC). However, proteins of the endocytic machinery are excluded from MCC. In a screen, we identified 28 genes affecting MCC appearance and found that genes involved in lipid biosynthesis and vesicle transport are significantly overrepresented. Deletion of Pil1, a component of eisosomes, or of Nce102, an integral membrane protein of MCC, results in the dissipation of all MCC markers. These deletion mutants also show accelerated endocytosis of MCC-resident permeases Can1 and Fur4. Our data suggest that release from MCC makes these proteins accessible to the endocytic machinery. Addition of arginine to wild-type cells leads to a similar redistribution and increased turnover of Can1. Thus, MCC represents a protective area within the plasma membrane to control turnover of transport proteins. |
format | Text |
id | pubmed-2600745 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-26007452009-06-15 Plasma membrane microdomains regulate turnover of transport proteins in yeast Grossmann, Guido Malinsky, Jan Stahlschmidt, Wiebke Loibl, Martin Weig-Meckl, Ina Frommer, Wolf B. Opekarová, Miroslava Tanner, Widmar J Cell Biol Research Articles In this study, we investigate whether the stable segregation of proteins and lipids within the yeast plasma membrane serves a particular biological function. We show that 21 proteins cluster within or associate with the ergosterol-rich membrane compartment of Can1 (MCC). However, proteins of the endocytic machinery are excluded from MCC. In a screen, we identified 28 genes affecting MCC appearance and found that genes involved in lipid biosynthesis and vesicle transport are significantly overrepresented. Deletion of Pil1, a component of eisosomes, or of Nce102, an integral membrane protein of MCC, results in the dissipation of all MCC markers. These deletion mutants also show accelerated endocytosis of MCC-resident permeases Can1 and Fur4. Our data suggest that release from MCC makes these proteins accessible to the endocytic machinery. Addition of arginine to wild-type cells leads to a similar redistribution and increased turnover of Can1. Thus, MCC represents a protective area within the plasma membrane to control turnover of transport proteins. The Rockefeller University Press 2008-12-15 /pmc/articles/PMC2600745/ /pubmed/19064668 http://dx.doi.org/10.1083/jcb.200806035 Text en © 2008 Grossmann et al. 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.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Grossmann, Guido Malinsky, Jan Stahlschmidt, Wiebke Loibl, Martin Weig-Meckl, Ina Frommer, Wolf B. Opekarová, Miroslava Tanner, Widmar Plasma membrane microdomains regulate turnover of transport proteins in yeast |
title | Plasma membrane microdomains regulate turnover of transport proteins in yeast |
title_full | Plasma membrane microdomains regulate turnover of transport proteins in yeast |
title_fullStr | Plasma membrane microdomains regulate turnover of transport proteins in yeast |
title_full_unstemmed | Plasma membrane microdomains regulate turnover of transport proteins in yeast |
title_short | Plasma membrane microdomains regulate turnover of transport proteins in yeast |
title_sort | plasma membrane microdomains regulate turnover of transport proteins in yeast |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2600745/ https://www.ncbi.nlm.nih.gov/pubmed/19064668 http://dx.doi.org/10.1083/jcb.200806035 |
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