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http://purl.uniprot.org/citations/12832401http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12832401http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12832401http://www.w3.org/2000/01/rdf-schema#comment"The Sec1p-like/Munc18 (SM) protein Munc18a binds to the neuronal t-SNARE Syntaxin1A and inhibits SNARE complex assembly. Tomosyn, a cytosolic Syntaxin1A-binding protein, is thought to regulate the interaction between Syntaxin1A and Munc18a, thus acting as a positive regulator of SNARE assembly. In the present study we have investigated the interaction between b-Tomosyn and the adipocyte SNARE complex involving Syntaxin4/SNAP23/VAMP-2 and the SM protein Munc18c, in vitro, and the potential involvement of Tomosyn in regulating the translocation of GLUT4 containing vesicles, in vivo. Tomosyn formed a high affinity ternary complex with Syntaxin4 and SNAP23 that was competitively inhibited by VAMP-2. Using a yeast two-hybrid assay we demonstrate that the VAMP-2-like domain in Tomosyn facilitates the interaction with Syntaxin4. Overexpression of Tomosyn in 3T3-L1 adipocytes inhibited the translocation of green fluorescent protein-GLUT4 to the plasma membrane. The SM protein Munc18c was shown to interact with the Syntaxin4 monomer, Syntaxin4 containing SNARE complexes, and the Syntaxin4/Tomosyn complex. These data suggest that Tomosyn and Munc18c operate at a similar stage of the Syntaxin4 SNARE assembly cycle, which likely primes Syntaxin4 for entry into the ternary SNARE complex."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m304261200"xsd:string
http://purl.uniprot.org/citations/12832401http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m304261200"xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"James D.E."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"James D.E."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Rea S."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Rea S."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Bryant N.J."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Bryant N.J."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Girotti M."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Girotti M."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Widberg C.H."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/author"Widberg C.H."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/pages"35093-35101"xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/pages"35093-35101"xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/title"Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/title"Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation."xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12832401http://purl.uniprot.org/core/volume"278"xsd:string