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http://purl.uniprot.org/citations/19064668http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19064668http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19064668http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200806035"xsd:string
http://purl.uniprot.org/citations/19064668http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200806035"xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Frommer W.B."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Frommer W.B."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Tanner W."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Tanner W."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Loibl M."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Loibl M."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Malinsky J."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Malinsky J."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Opekarova M."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Opekarova M."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Grossmann G."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Grossmann G."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Stahlschmidt W."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Stahlschmidt W."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Weig-Meckl I."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/author"Weig-Meckl I."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/19064668http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string