RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/12529442http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12529442http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12529442http://www.w3.org/2000/01/rdf-schema#comment"VCP/p97 is involved in a variety of cellular processes, including membrane fusion and ubiquitin-dependent protein degradation. It has been suggested that adaptor proteins such as p47 and Ufd1p confer functional versatility to VCP/p97. To identify novel adaptors, we searched for proteins that interact specifically with VCP/p97 by using the yeast two-hybrid system, and discovered a novel VCP/p97-interacting protein named small VCP/p97-interacting protein (SVIP). Rat SVIP is a 76-amino acid protein that contains two putative coiled-coil regions, and potential myristoylation and palmitoylation sites at the N terminus. Binding experiments revealed that the N-terminal coiled-coil region of SVIP, and the N-terminal and subsequent ATP-binding regions (ND1 domain) of VCP/p97, interact with each other. SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner. Overexpression of full-length SVIP or a truncated mutant did not markedly affect the structure of the Golgi apparatus, but caused extensive cell vacuolation reminiscent of that seen upon the expression of VCP/p97 mutants or polyglutamine proteins in neuronal cells. The vacuoles seemed to be derived from endoplasmic reticulum membranes. These results together suggest that SVIP is a novel VCP/p97 adaptor whose function is related to the integrity of the endoplasmic reticulum."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.org/dc/terms/identifier"doi:10.1091/mbc.02-07-0115"xsd:string
http://purl.uniprot.org/citations/12529442http://purl.org/dc/terms/identifier"doi:10.1091/mbc.02-07-0115"xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Hamada Y."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Hamada Y."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Tani K."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Tani K."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Hatsuzawa K."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Hatsuzawa K."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Tagaya M."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Tagaya M."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Nagahama M."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/author"Nagahama M."xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/pages"262-273"xsd:string
http://purl.uniprot.org/citations/12529442http://purl.uniprot.org/core/pages"262-273"xsd:string