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http://purl.uniprot.org/citations/9647643http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9647643http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9647643http://www.w3.org/2000/01/rdf-schema#comment"ER-to-Golgi transport, and perhaps intraGolgi transport involves a set of interacting soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins including syntaxin 5, GOS-28, membrin, rsec22b, and rbet1. By immunoelectron microscopy we find that rsec22b and rbet1 are enriched in COPII-coated vesicles that bud from the ER and presumably fuse with nearby vesicular tubular clusters (VTCs). However, all of the SNAREs were found on both COPII- and COPI-coated membranes, indicating that similar SNARE machinery directs both vesicle pathways. rsec22b and rbet1 do not appear beyond the first Golgi cisterna, whereas syntaxin 5 and membrin penetrate deeply into the Golgi stacks. Temperature shifts reveal that membrin, rsec22b, rbet1, and syntaxin 5 are present together on membranes that rapidly recycle between peripheral and Golgi-centric locations. GOS-28, on the other hand, maintains a fixed localization in the Golgi. By immunoprecipitation analysis, syntaxin 5 exists in at least two major subcomplexes: one containing syntaxin 5 (34-kD isoform) and GOS-28, and another containing syntaxin 5 (41- and 34-kD isoforms), membrin, rsec22b, and rbet1. Both subcomplexes appear to involve direct interactions of each SNARE with syntaxin 5. Our results indicate a central role for complexes among rbet1, rsec22b, membrin, and syntaxin 5 (34 and 41 kD) at two membrane fusion interfaces: the fusion of ER-derived vesicles with VTCs, and the assembly of VTCs to form cis-Golgi elements. The 34-kD syntaxin 5 isoform, membrin, and GOS-28 may function in intraGolgi transport."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.org/dc/terms/identifier"doi:10.1083/jcb.141.7.1489"xsd:string
http://purl.uniprot.org/citations/9647643http://purl.org/dc/terms/identifier"doi:10.1083/jcb.141.7.1489"xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Scheller R.H."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Scheller R.H."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Klumperman J."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Klumperman J."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Oorschot V."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Oorschot V."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Hay J.C."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Hay J.C."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Steegmaier M."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Steegmaier M."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Kuo C.S."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/author"Kuo C.S."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/pages"1489-1502"xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/pages"1489-1502"xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/title"Localization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREs."xsd:string
http://purl.uniprot.org/citations/9647643http://purl.uniprot.org/core/title"Localization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREs."xsd:string