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Plasma membrane polarization during mating in yeast cells

The yeast mating cell provides a simple paradigm for analyzing mechanisms underlying the generation of surface polarity. Endocytic recycling and slow diffusion on the plasma membrane were shown to facilitate polarized surface distribution of Snc1p (Valdez-Taubas, J., and H.R. Pelham. 2003. Curr. Bio...

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Detalles Bibliográficos
Autores principales: Proszynski, Tomasz J., Klemm, Robin, Bagnat, Michel, Gaus, Katharina, Simons, Kai
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063912/
https://www.ncbi.nlm.nih.gov/pubmed/16769822
http://dx.doi.org/10.1083/jcb.200602007
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author Proszynski, Tomasz J.
Klemm, Robin
Bagnat, Michel
Gaus, Katharina
Simons, Kai
author_facet Proszynski, Tomasz J.
Klemm, Robin
Bagnat, Michel
Gaus, Katharina
Simons, Kai
author_sort Proszynski, Tomasz J.
collection PubMed
description The yeast mating cell provides a simple paradigm for analyzing mechanisms underlying the generation of surface polarity. Endocytic recycling and slow diffusion on the plasma membrane were shown to facilitate polarized surface distribution of Snc1p (Valdez-Taubas, J., and H.R. Pelham. 2003. Curr. Biol. 13:1636–1640). Here, we found that polarization of Fus1p, a raft-associated type I transmembrane protein involved in cell fusion, does not depend on endocytosis. Instead, Fus1p localization to the tip of the mating projection was determined by its cytosolic domain, which binds to peripheral proteins involved in mating tip polarization. Furthermore, we provide evidence that the lipid bilayer at the mating projection is more condensed than the plasma membrane enclosing the cell body, and that sphingolipids are required for this lipid organization.
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spelling pubmed-20639122007-11-29 Plasma membrane polarization during mating in yeast cells Proszynski, Tomasz J. Klemm, Robin Bagnat, Michel Gaus, Katharina Simons, Kai J Cell Biol Research Articles The yeast mating cell provides a simple paradigm for analyzing mechanisms underlying the generation of surface polarity. Endocytic recycling and slow diffusion on the plasma membrane were shown to facilitate polarized surface distribution of Snc1p (Valdez-Taubas, J., and H.R. Pelham. 2003. Curr. Biol. 13:1636–1640). Here, we found that polarization of Fus1p, a raft-associated type I transmembrane protein involved in cell fusion, does not depend on endocytosis. Instead, Fus1p localization to the tip of the mating projection was determined by its cytosolic domain, which binds to peripheral proteins involved in mating tip polarization. Furthermore, we provide evidence that the lipid bilayer at the mating projection is more condensed than the plasma membrane enclosing the cell body, and that sphingolipids are required for this lipid organization. The Rockefeller University Press 2006-06-19 /pmc/articles/PMC2063912/ /pubmed/16769822 http://dx.doi.org/10.1083/jcb.200602007 Text en Copyright © 2006, 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
Proszynski, Tomasz J.
Klemm, Robin
Bagnat, Michel
Gaus, Katharina
Simons, Kai
Plasma membrane polarization during mating in yeast cells
title Plasma membrane polarization during mating in yeast cells
title_full Plasma membrane polarization during mating in yeast cells
title_fullStr Plasma membrane polarization during mating in yeast cells
title_full_unstemmed Plasma membrane polarization during mating in yeast cells
title_short Plasma membrane polarization during mating in yeast cells
title_sort plasma membrane polarization during mating in yeast cells
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063912/
https://www.ncbi.nlm.nih.gov/pubmed/16769822
http://dx.doi.org/10.1083/jcb.200602007
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