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http://purl.uniprot.org/citations/18508925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18508925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18508925http://www.w3.org/2000/01/rdf-schema#comment"Glucose-dependent regulation of carbon metabolism is a subject of intensive studies. We have previously shown that the switch from gluconeogenesis to glycolysis is associated with ubiquitin-proteasome linked elimination of the key enzyme fructose-1,6-bisphosphatase. Seven glucose induced degradation deficient (Gid)-proteins found previously in a genomic screen were shown to form a complex that binds FBPase. One of the subunits, Gid2/Rmd5, contains a degenerated RING finger domain. In an in vitro assay, heterologous expression of GST-Gid2 leads to polyubiquitination of proteins. In addition, we show that a mutation in the degenerated RING domain of Gid2/Rmd5 abolishes fructose-1,6-bisphosphatase polyubiquitination and elimination in vivo. Six Gid proteins are present in gluconeogenic cells. A seventh protein, Gid4/Vid24, occurs upon glucose addition to gluconeogenic cells and is afterwards eliminated. Forcing abnormal expression of Gid4/Vid24 in gluconeogenic cells leads to fructose-1,6-bisphosphatase degradation. This suggests that Gid4/Vid24 initiates fructose-1,6-bisphosphatase polyubiquitination by the Gid complex and its subsequent elimination by the proteasome. We also show that an additional gluconeogenic enzyme, phosphoenolpyruvate carboxykinase, is subject to Gid complex-dependent degradation. Our study uncovers a new type of ubiquitin ligase complex composed of novel subunits involved in carbohydrate metabolism and identifies Gid4/Vid24 as a major regulator of this E3."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e08-03-0328"xsd:string
http://purl.uniprot.org/citations/18508925http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e08-03-0328"xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Hofmann K."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Hofmann K."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Wolf D.H."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Wolf D.H."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Braun B."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Braun B."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Thumm M."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Thumm M."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Scheel H."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Scheel H."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Juretschke J."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Juretschke J."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Kimmig P."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Kimmig P."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Pfirrmann T."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Pfirrmann T."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Santt O."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/author"Santt O."xsd:string
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18508925http://purl.uniprot.org/core/date"2008"xsd:gYear