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http://purl.uniprot.org/citations/8128252 | http://www.w3.org/2000/01/rdf-schema#comment | "Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals."xsd:string |
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http://purl.uniprot.org/citations/8128252 | http://purl.uniprot.org/core/author | "Cosson P."xsd:string |
http://purl.uniprot.org/citations/8128252 | http://purl.uniprot.org/core/author | "Letourneur F."xsd:string |
http://purl.uniprot.org/citations/8128252 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
http://purl.uniprot.org/citations/8128252 | http://purl.uniprot.org/core/name | "Science"xsd:string |
http://purl.uniprot.org/citations/8128252 | http://purl.uniprot.org/core/pages | "1629-1631"xsd:string |
http://purl.uniprot.org/citations/8128252 | http://purl.uniprot.org/core/title | "Coatomer interaction with di-lysine endoplasmic reticulum retention motifs."xsd:string |
http://purl.uniprot.org/citations/8128252 | http://purl.uniprot.org/core/volume | "263"xsd:string |
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