Plasma membrane microdomains regulate turnover of transport proteins in yeast
Autor: | Miroslava Opekarová, Ina Weig-Meckl, Jan Malinsky, Wolf B. Frommer, Guido Grossmann, Wiebke Stahlschmidt, Martin Loibl, Widmar Tanner |
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Rok vydání: | 2008 |
Předmět: |
Saccharomyces cerevisiae Proteins
Octoxynol Recombinant Fusion Proteins Endocytic cycle Green Fluorescent Proteins Saccharomyces cerevisiae Models Biological Article Cell membrane 03 medical and health sciences 0302 clinical medicine Membrane Microdomains medicine Integral membrane protein Eisosome Research Articles 030304 developmental biology Cell Proliferation 0303 health sciences Genes Essential biology Membrane transport protein Permease food and beverages Cell Biology Endocytosis Cell biology Transport protein Vesicular transport protein medicine.anatomical_structure Mutation biology.protein Amino Acid Transport Systems Basic Genome Fungal Carrier Proteins Protein Processing Post-Translational 030217 neurology & neurosurgery Biomarkers |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 |
Popis: | 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. |
Databáze: | OpenAIRE |
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