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http://purl.uniprot.org/citations/14583093http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14583093http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14583093http://www.w3.org/2000/01/rdf-schema#comment"Snf7p (sucrose non-fermenting) and Vps20p (vacuolar protein-sorting) are small coil-coiled proteins involved in yeast MVB (multivesicular body) structure, formation and function. In the present study, we report the identification of three human homologues of yeast Snf7p, designated hSnf7-1, hSnf7-2 and hSnf7-3, and a single human Vps20p homologue, designated hVps20, that may have similar roles in humans. Immunofluorescence studies showed that hSnf7-1 and hSnf7-3 localized in large vesicular structures that also co-localized with late endosomal/lysosomal structures induced by overexpressing an ATPase-defective Vps4-A mutant. In contrast, overexpressed hVps20 showed a typical endosomal membrane-staining pattern, and co-expression of hVps20 with Snf7-1 dispersed the large Snf7-staining vesicles. Interestingly, overexpression of both hSnf7 and hVps20 proteins induced a post-endosomal defect in cholesterol sorting. To explore possible protein-protein interactions involving hSnf7 proteins, we used information from yeast genomic studies showing that yeast Snf7p can interact with proteins involved in MVB function. Using a glutathione S-transferase-capture approach with several mammalian homologues of such yeast Snf7p-interacting proteins, we found that all three hSnf7s interacted with mouse AIP1 [ALG-2 (apoptosis-linked gene 2) interacting protein 1], a mammalian Bro1p [BCK1 (bypass of C kinase)-like resistance to osmotic shock]-containing protein involved in cellular vacuolization and apoptosis. Whereas mapping experiments showed that the N-terminus of AIP1 containing both a Bro1 and an alpha-helical domain were required for interaction with hSnf7-1, Snf7-1 did not interact with another human Bro1-containing molecule, rhophilin-2. Co-immunoprecipitation experiments confirmed the in vivo interaction of hSnf7-1 and AIP1. Additional immunofluorescence experiments showed that hSnf7-1 recruited cytosolic AIP1 to the Snf7-induced vacuolar-like structures. Together these results suggest that mammalian Vps20, AIP1 and Snf7 proteins, like their yeast counterparts, play roles in MVB function."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.org/dc/terms/identifier"doi:10.1042/bj20031347"xsd:string
http://purl.uniprot.org/citations/14583093http://purl.org/dc/terms/identifier"doi:10.1042/bj20031347"xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/author"Bowden E.T."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/author"Bowden E.T."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/author"Burbelo P.D."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/author"Burbelo P.D."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/author"Peck J.W."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/author"Peck J.W."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/pages"693-700"xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/pages"693-700"xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/title"Structure and function of human Vps20 and Snf7 proteins."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/title"Structure and function of human Vps20 and Snf7 proteins."xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/volume"377"xsd:string
http://purl.uniprot.org/citations/14583093http://purl.uniprot.org/core/volume"377"xsd:string
http://purl.uniprot.org/citations/14583093http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14583093
http://purl.uniprot.org/citations/14583093http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14583093
http://purl.uniprot.org/citations/14583093http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14583093
http://purl.uniprot.org/citations/14583093http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14583093
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