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http://purl.uniprot.org/citations/16452633http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16452633http://www.w3.org/2000/01/rdf-schema#comment"Gcs1 is an Arf GTPase-activating protein (Arf-GAP) that mediates Golgi-ER and post-Golgi vesicle transport in yeast. Here we show that the Snc1,2 v-SNAREs, which mediate endocytosis and exocytosis, interact physically and genetically with Gcs1. Moreover, Gcs1 and the Snc v-SNAREs colocalize to subcellular structures that correspond to the trans-Golgi and endosomal compartments. Studies performed in vitro demonstrate that the Snc-Gcs1 interaction results in the efficient binding of recombinant Arf1Delta17N-Q71L to the v-SNARE and the recruitment of purified coatomer. In contrast, the presence of Snc had no effect on Gcs1 Arf-GAP activity in vitro, suggesting that v-SNARE binding does not attenuate Arf1 function. Disruption of both the SNC and GCS1 genes results in synthetic lethality, whereas overexpression of either SNC gene inhibits the growth of a distinct subset of COPI mutants. We show that GFP-Snc1 recycling to the trans-Golgi is impaired in gcs1Delta cells and these COPI mutants. Together, these results suggest that Gcs1 facilitates the incorporation of the Snc v-SNAREs into COPI recycling vesicles and subsequent endosome-Golgi sorting in yeast."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e05-09-0832"xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Spang A."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Robinson M."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Schindler C."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Gerst J.E."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Kama R."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Gabriely G."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Johnston G.C."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Poon P.P."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Singer R.A."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/author"Murray L.E."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/name"Mol Biol Cell"xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/pages"1845-1858"xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/title"The Gcs1 Arf-GAP mediates Snc1,2 v-SNARE retrieval to the Golgi in yeast."xsd:string
http://purl.uniprot.org/citations/16452633http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/16452633http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16452633
http://purl.uniprot.org/citations/16452633http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16452633
http://purl.uniprot.org/uniprot/P35197#attribution-D9BB12827BA59F4AA5F5EA4FBC86A6BAhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16452633
http://purl.uniprot.org/uniprot/P31109#attribution-D9BB12827BA59F4AA5F5EA4FBC86A6BAhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16452633
http://purl.uniprot.org/uniprot/P33328#attribution-D9BB12827BA59F4AA5F5EA4FBC86A6BAhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16452633
http://purl.uniprot.org/uniprot/#_P31109-mappedCitation-16452633http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16452633
http://purl.uniprot.org/uniprot/#_P33328-mappedCitation-16452633http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16452633