http://purl.uniprot.org/citations/14699056 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/14699056 | http://www.w3.org/2000/01/rdf-schema#comment | "Coatomer is required for the retrieval of proteins from an early Golgi compartment back to the endoplasmic reticulum. The WD40 domain of alpha-COP is required for the recruitment of KKTN-tagged proteins into coatomer-coated vesicles. However, lack of the domain has only minor effects on growth in yeast. Here, we show that the WD40 domain of beta'-COP is required for the recycling of the KTKLL-tagged Golgi protein Emp47p. The protein is degraded more rapidly in cells with a point mutation in the WD40 domain of beta'-COP (sec27-95) or in cells lacking the domain altogether, whereas a point mutation in the Clathrin Heavy Chain Repeat (sec27-1) does not affect the turnover of Emp47p. Lack of the WD40 domain of beta'-COP has only minor effects on growth of yeast cells; however, absence of both WD40 domains of alpha- and beta'-COP is lethal. Two hybrid studies together with our analysis of the maturation of KKTN-tagged invertase and the turnover of Emp47p in alpha- and beta'-COP mutants suggest that the two WD40 domains of alpha- and beta'-COP bind distinct but overlapping sets of di-lysine signals and hence both contribute to recycling of proteins with di-lysine signals."xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e03-10-0724"xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/author | "Dale M."xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/author | "Duden R."xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/author | "Frigerio G."xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/author | "Eugster A."xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/name | "Mol Biol Cell"xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/pages | "1011-1023"xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/title | "The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs."xsd:string |
http://purl.uniprot.org/citations/14699056 | http://purl.uniprot.org/core/volume | "15"xsd:string |
http://purl.uniprot.org/citations/14699056 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14699056 |
http://purl.uniprot.org/citations/14699056 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/14699056 |
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http://purl.uniprot.org/uniprot/P43555 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14699056 |
http://purl.uniprot.org/uniprot/P32074 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14699056 |
http://purl.uniprot.org/uniprot/P40509 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14699056 |