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http://purl.uniprot.org/citations/11157748http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11157748http://www.w3.org/2000/01/rdf-schema#comment"The role of protein phosphorylation in secretion is not well understood. Here we show that yeast lacking the Snc1,2 v-SNAREs, or bearing a temperature-sensitive mutation in the Sso2 t-SNARE, are rescued at restrictive conditions by the addition of ceramide precursors and analogs to the growth medium. Rescue results from dephosphorylation of the Sso t-SNAREs by a ceramide-activated type 2A protein phosphatase (Sit4) involved in cell cycle control. Sso t-SNARE dephosphorylation correlated with its assembly into complexes with the Sec9 t-SNARE, both in vitro and in vivo, and with an increase in protein trafficking and secretion in cells. SNARE complexes isolated under these conditions contained only Sso and Sec9, suggesting that a t-t-SNARE fusion complex is sufficient to confer exocytosis. Mutation of a single PKA site (Ser79 to Ala79) in Sso1 resulted in a decrease in phosphorylation and was sufficient to confer growth to snc cells at restrictive conditions. Thus, modulation of t-SNARE phosphorylation regulates SNARE complex assembly and membrane fusion in vivo."xsd:string
http://purl.uniprot.org/citations/11157748http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.3.411"xsd:string
http://purl.uniprot.org/citations/11157748http://purl.uniprot.org/core/author"Gerst J.E."xsd:string
http://purl.uniprot.org/citations/11157748http://purl.uniprot.org/core/author"Marash M."xsd:string
http://purl.uniprot.org/citations/11157748http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11157748http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/11157748http://purl.uniprot.org/core/pages"411-421"xsd:string
http://purl.uniprot.org/citations/11157748http://purl.uniprot.org/core/title"t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast."xsd:string
http://purl.uniprot.org/citations/11157748http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/11157748http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11157748
http://purl.uniprot.org/citations/11157748http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11157748
http://purl.uniprot.org/uniprot/#_P39926-mappedCitation-11157748http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11157748
http://purl.uniprot.org/uniprot/#_P40357-mappedCitation-11157748http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11157748
http://purl.uniprot.org/uniprot/#_P32867-mappedCitation-11157748http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11157748
http://purl.uniprot.org/uniprot/P32867http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11157748
http://purl.uniprot.org/uniprot/P40357http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11157748
http://purl.uniprot.org/uniprot/P39926http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11157748