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http://purl.uniprot.org/citations/11062261http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11062261http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11062261http://www.w3.org/2000/01/rdf-schema#comment"Rab5 regulates endocytic membrane traffic by specifically recruiting cytosolic effector proteins to their site of action on early endosomal membranes. We have characterized a new Rab5 effector complex involved in endosomal fusion events. This complex includes a novel protein, Rabenosyn-5, which, like the previously characterized Rab5 effector early endosome antigen 1 (EEA1), contains an FYVE finger domain and is recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. Rabenosyn-5 is complexed to the Sec1-like protein hVPS45. hVPS45 does not interact directly with Rab5, therefore Rabenosyn-5 serves as a molecular link between hVPS45 and the Rab5 GTPase. This property suggests that Rabenosyn-5 is a closer mammalian functional homologue of yeast Vac1p than EEA1. Furthermore, although both EEA1 and Rabenosyn-5 are required for early endosomal fusion, only overexpression of Rabenosyn-5 inhibits cathepsin D processing, suggesting that the two proteins play distinct roles in endosomal trafficking. We propose that Rab5-dependent formation of membrane domains enriched in phosphatidylinositol-3-phosphate has evolved as a mechanism for the recruitment of multiple effector proteins to mammalian early endosomes, and that these domains are multifunctional, depending on the differing activities of the effector proteins recruited."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.org/dc/terms/identifier"doi:10.1083/jcb.151.3.601"xsd:string
http://purl.uniprot.org/citations/11062261http://purl.org/dc/terms/identifier"doi:10.1083/jcb.151.3.601"xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Wilm M."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Wilm M."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Nielsen E."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Nielsen E."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Christoforidis S."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Christoforidis S."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Uttenweiler-Joseph S."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Uttenweiler-Joseph S."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Zerial M."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Zerial M."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Miaczynska M."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Miaczynska M."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Dewitte F."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Dewitte F."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Hoflack B."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/author"Hoflack B."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/11062261http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string