RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/8858162http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8858162http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8858162http://www.w3.org/2000/01/rdf-schema#comment"Coatomer is a cytosolic protein complex that forms the coat of COP I-coated transport vesicles. In our attempt to analyze the physical and functional interactions between its seven subunits (coat proteins, [COPs] alpha-zeta), we engaged in a program to clone and characterize the individual coatomer subunits. We have now cloned, sequenced, and overexpressed bovine alpha-COP, the 135-kD subunit of coatomer as well as delta-COP, the 57-kD subunit and have identified a yeast homolog of delta-COP by cDNA sequence comparison and by NH2-terminal peptide sequencing. delta-COP shows homologies to subunits of the clathrin adaptor complexes AP1 and AP2. We show that in Golgi-enriched membrane fractions, the protein is predominantly found in COP I-coated transport vesicles and in the budding regions of the Golgi membranes. A knock-out of the delta-COP gene in yeast is lethal. Immunoprecipitation, as well as analysis exploiting the two-hybrid system in a complete COP screen, showed physical interactions between alpha- and epsilon-COPs and between beta- and delta-COPs. Moreover, the two-hybrid system indicates interactions between gamma- and zeta-COPs as well as between alpha- and beta' COPs. We propose that these interactions reflect in vivo associations of those subunits and thus play a functional role in the assembly of coatomer and/or serve to maintain the molecular architecture of the complex."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.org/dc/terms/identifier"doi:10.1083/jcb.135.1.53"xsd:string
http://purl.uniprot.org/citations/8858162http://purl.org/dc/terms/identifier"doi:10.1083/jcb.135.1.53"xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Lottspeich F."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Lottspeich F."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Wieland F.T."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Wieland F.T."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Orci L."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Orci L."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Ravazzola M."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Ravazzola M."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Tschochner H."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Tschochner H."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Harter C."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Harter C."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Stenbeck G."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Stenbeck G."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Auerbach S."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Auerbach S."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Faulstich D."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Faulstich D."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Wegehingel S."xsd:string
http://purl.uniprot.org/citations/8858162http://purl.uniprot.org/core/author"Wegehingel S."xsd:string