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http://purl.uniprot.org/citations/11707266http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11707266http://www.w3.org/2000/01/rdf-schema#comment"Caveolins are scaffolding proteins able to collect on caveolae a large number of signalling proteins bearing a caveolin-binding motif. The proteins of the striatin family, striatin, SG2NA, and zinedin, are composed of several conserved, collinearly aligned, protein-protein association domains, among which a putative caveolin-binding domain [Castets et al. (2000) J. Biol. Chem. 275, 19970-19977]. They are associated in part with membranes. These proteins are mainly expressed within neurons and thought to act both as scaffolds and as Ca(2+)-dependent signalling proteins [Bartoli et al. (1999) J. Neurobiol. 40, 234-243]. Here, we show that (1) rat brain striatin, SG2NA and zinedin co-immunoprecipitate with caveolin-1; (2) all are pulled down by glutathione-S-transferase (GST)-caveolin-1; (3) a fragment of recombinant striatin containing the putative caveolin-binding domain binds GST-caveolin-1. Hence, it is likely that the proteins of the striatin family are addressed to membrane microdomains by their binding to caveolin, in accordance with their putative role in membrane trafficking [Baillat et al. (2001) Mol. Biol. Cell 12, 663-673]."xsd:string
http://purl.uniprot.org/citations/11707266http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(01)03020-4"xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/author"Gaillard S."xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/author"Castets F."xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/author"Monneron A."xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/author"Bartoli M."xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/pages"49-52"xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/title"Striatin, a calmodulin-dependent scaffolding protein, directly binds caveolin-1."xsd:string
http://purl.uniprot.org/citations/11707266http://purl.uniprot.org/core/volume"508"xsd:string
http://purl.uniprot.org/citations/11707266http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11707266
http://purl.uniprot.org/citations/11707266http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11707266
http://purl.uniprot.org/uniprot/#_P70483-mappedCitation-11707266http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11707266
http://purl.uniprot.org/uniprot/#_A0A8I6AG38-mappedCitation-11707266http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11707266
http://purl.uniprot.org/uniprot/#_G3V6L8-mappedCitation-11707266http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11707266
http://purl.uniprot.org/uniprot/A0A8I6AG38http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11707266
http://purl.uniprot.org/uniprot/P70483http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11707266
http://purl.uniprot.org/uniprot/G3V6L8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11707266