RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/8376457http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8376457http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8376457http://www.w3.org/2000/01/rdf-schema#comment"Using a novel in vitro assay which allows us to distinguish vesicle budding from subsequent targeting and fusion steps, we provide the first biological evidence that beta-COP, a component of non-clathrin-coated vesicles believed to mediate intraGolgi transport, is essential for transport of protein from the ER to the cis-Golgi compartment. Incubation in the presence of beta-COP specific antibodies and F(ab) fragments prevents the exit of vesicular stomatitis virus glycoprotein (VSV-G) from the ER. These results demonstrate that beta-COP is required for the assembly of coat complexes mediating vesicle budding. Fractionation of rat liver cytosol revealed that a major biologically active form of beta-COP was found in a high molecular pool (> 1,000 kD) distinct from coatomer and which promoted efficient vesicle budding from the ER. Surprisingly, rab1B could be quantitatively coprecipitated with this beta-COP containing complex and was also essential for function. We suggest that beta-COP functions in an early step during vesicle formation and that rab1B may be recruited as a component of a precoat complex which participates in the export of protein from the ER via vesicular carriers."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.org/dc/terms/identifier"doi:10.1083/jcb.122.6.1155"xsd:string
http://purl.uniprot.org/citations/8376457http://purl.org/dc/terms/identifier"doi:10.1083/jcb.122.6.1155"xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Zhu H."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Zhu H."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Peter F."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Peter F."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Balch W.E."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Balch W.E."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Kreis T.E."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Kreis T.E."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Plutner H."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/author"Plutner H."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/pages"1155-1167"xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/pages"1155-1167"xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/title"Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/title"Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro."xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/volume"122"xsd:string
http://purl.uniprot.org/citations/8376457http://purl.uniprot.org/core/volume"122"xsd:string