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http://purl.uniprot.org/citations/8846786http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8846786http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8846786http://www.w3.org/2000/01/rdf-schema#comment"Protein phosphatase type 1 (PP1) is encoded by GLC7, an essential gene in Saccharomyces cerevisiae. The GLC7 phosphatase is required for glucose repression and appears to function antagonistically to the SNF1 protein kinase. Previously, we characterized a mutation, glc7-T152K, that relieves glucose repression but does not interfere with the function of GLC7 in glycogen metabolism. We proposed that the mutant GLC7T152K phosphatase is defective in its interaction with a regulatory subunit that directs participation of PP1 in the glucose repression mechanism. Here, we present evidence that REG1, a protein required for glucose repression, is one such regulatory subunit. We show that REG1 is physically associated with GLC7. REG1 interacts with GLC7 strongly and specifically in the two-hybrid system, and REG1 and GLC7 fusion proteins co-immunoprecipitate from cell extracts. Moreover, overexpression of a REG1 fusion protein suppresses the glc7-T152K mutant defect in glucose repression. This and other genetic evidence indicate that the two proteins function together in regulating glucose repression. These results suggest that REG1 is a regulatory subunit of PP1 that targets its activity to proteins in the glucose repression regulatory pathway."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1995.tb00282.x"xsd:string
http://purl.uniprot.org/citations/8846786http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1995.tb00282.x"xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/author"Carlson M."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/author"Carlson M."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/author"Tu J.L."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/author"Tu J.L."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/pages"5939-5946"xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/pages"5939-5946"xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/title"REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/title"REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/8846786http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/8846786http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8846786
http://purl.uniprot.org/citations/8846786http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8846786
http://purl.uniprot.org/citations/8846786http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8846786
http://purl.uniprot.org/citations/8846786http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8846786
http://purl.uniprot.org/uniprot/Q00816http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8846786
http://purl.uniprot.org/uniprot/Q00816#attribution-D55757C136889841E341D068EE67445Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8846786