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http://purl.uniprot.org/citations/10021387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10021387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10021387http://www.w3.org/2000/01/rdf-schema#comment"The vacuolar protein sorting (VPS) pathway of Saccharomyces cerevisiae mediates transport of vacuolar protein precursors from the late Golgi to the lysosome-like vacuole. Sorting of some vacuolar proteins occurs via a prevacuolar endosomal compartment and mutations in a subset of VPS genes (the class D VPS genes) interfere with the Golgi-to-endosome transport step. Several of the encoded proteins, including Pep12p/Vps6p (an endosomal target (t) SNARE) and Vps45p (a Sec1p homologue), bind each other directly [1]. Another of these proteins, Vac1p/Pep7p/Vps19p, associates with Pep12p and binds phosphatidylinositol 3-phosphate (PI(3)P), the product of the Vps34 phosphatidylinositol 3-kinase (PI 3-kinase) [1] [2]. Here, we demonstrate that Vac1p genetically and physically interacts with the activated, GTP-bound form of Vps21p, a Rab GTPase that functions in Golgi-to-endosome transport, and with Vps45p. These results implicate Vac1p as an effector of Vps21p and as a novel Sec1p-family-binding protein. We suggest that Vac1p functions as a multivalent adaptor protein that ensures the high fidelity of vesicle docking and fusion by integrating both phosphoinositide (Vps34p) and GTPase (Vps21p) signals, which are essential for Pep12p- and Vps45p-dependent targeting of Golgi-derived vesicles to the prevacuolar endosome."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.org/dc/terms/identifier"doi:10.1016/s0960-9822(99)80071-2"xsd:string
http://purl.uniprot.org/citations/10021387http://purl.org/dc/terms/identifier"doi:10.1016/s0960-9822(99)80071-2"xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/author"Emr S.D."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/author"Emr S.D."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/author"Burd C.G."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/author"Burd C.G."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/author"Peterson M.R."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/author"Peterson M.R."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/pages"159-162"xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/pages"159-162"xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/title"Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/title"Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome."xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/10021387http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/10021387http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10021387
http://purl.uniprot.org/citations/10021387http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10021387
http://purl.uniprot.org/citations/10021387http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10021387
http://purl.uniprot.org/citations/10021387http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10021387