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http://purl.uniprot.org/citations/10788491http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10788491http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10788491http://www.w3.org/2000/01/rdf-schema#comment"Members of the syntaxin family are target-soluble N-ethylmaleimide-sensitive factor-attachment protein receptors involved in vesicle docking and/or fusion within the exocytic and endocytotic pathways. By using the yeast two-hybrid system, we have identified a novel member of the syntaxin family, syntaxin 18, that binds to alpha-soluble N-ethylmaleimide-sensitive factor-attachment protein. Subcellular fractionation and immunocytochemical analysis revealed that syntaxin 18 is principally located in the endoplasmic reticulum. We examined the effect of overexpression of FLAG-tagged syntaxin 18 and a mutant lacking the N-terminal 81 amino acid residues on protein transport and organelles in the early secretory pathway. Both expressed proteins localized to the endoplasmic reticulum, and the expressed FLAG-syntaxin 18 caused remarkable aggregation of endoplasmic reticulum membranes. Although expression of the FLAG-syntaxin 18 lacking the N-terminal region produced less effect on the morphology of the endoplasmic reticulum, dispersion of the endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi was elicited. Moreover, overexpression of the FLAG-syntaxin 18 mutant inhibited protein export from the endoplasmic reticulum. These results taken together suggest that syntaxin 18 functions in transport between the endoplasmic reticulum and Golgi."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.18.13713"xsd:string
http://purl.uniprot.org/citations/10788491http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.18.13713"xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Scheller R.H."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Scheller R.H."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Hirose H."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Hirose H."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Tani K."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Tani K."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Hatsuzawa K."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Hatsuzawa K."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Tagaya M."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/author"Tagaya M."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/pages"13713-13720"xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/pages"13713-13720"xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/title"Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking."xsd:string
http://purl.uniprot.org/citations/10788491http://purl.uniprot.org/core/title"Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking."xsd:string