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...
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| Main Author: | |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
December 8, 2008
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| In: |
The journal of cell biology
Year: 2008, Volume: 183, Issue: 6, Pages: 1075-1088 |
| ISSN: | 1540-8140 |
| DOI: | 10.1083/jcb.200806035 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1083/jcb.200806035 Verlag, kostenfrei, Volltext: http://jcb.rupress.org/content/183/6/1075 
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| Author Notes: | Guido Grossmann, Jan Malinsky, Wiebke Stahlschmidt, Martin Loibl, Ina Weig-Meckl, Wolf B. Frommer, Miroslava Opekarová, and Widmar Tanner |
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| 520 | |a 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. | ||
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