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http://purl.uniprot.org/citations/25869668http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25869668http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25869668http://www.w3.org/2000/01/rdf-schema#comment"The recruitment of inositol phosphatases to endocytic membranes mediates dephosphorylation of PI(4,5)P2, a phosphoinositide concentrated in the plasma membrane, and prevents its accumulation on endosomes. The importance of the conversion of PI(4,5)P2 to PtdIns during endocytosis is demonstrated by the presence of both a 5-phosphatase and a 4-phosphatase (Sac domain) module in the synaptojanins, endocytic PI(4,5)P2 phosphatases conserved from yeast to humans and the only PI(4,5)P2 phosphatases in yeast. OCRL, another 5-phosphatase that couples endocytosis to PI(4,5)P2 dephosphorylation, lacks a Sac domain. Here we show that Sac2/INPP5F is a PI4P phosphatase that colocalizes with OCRL on endocytic membranes, including vesicles formed by clathrin-mediated endocytosis, macropinosomes, and Rab5 endosomes. An OCRL-Sac2/INPP5F interaction could be demonstrated by coimmunoprecipitation and was potentiated by Rab5, whose activity is required to recruit Sac2/INPP5F to endosomes. Sac2/INPP5F and OCRL may cooperate in the sequential dephosphorylation of PI(4,5)P2 at the 5 and 4 position of inositol in a partnership that mimics that of the two phosphatase modules of synaptojanin."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201409064"xsd:string
http://purl.uniprot.org/citations/25869668http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201409064"xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Zou Y."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Zou Y."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"De Camilli P."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"De Camilli P."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Nakatsu F."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Nakatsu F."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Strittmatter S.M."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Strittmatter S.M."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Messa M."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Messa M."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Czapla H."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Czapla H."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Nandez R."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/author"Nandez R."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/pages"85-95"xsd:string
http://purl.uniprot.org/citations/25869668http://purl.uniprot.org/core/pages"85-95"xsd:string