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http://purl.uniprot.org/citations/18182384http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18182384http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18182384http://www.w3.org/2000/01/rdf-schema#comment"In Saccharomyces cerevisiae, protein O-mannosylation, which is executed by protein O-mannosyltransferases, is essential for a variety of biological processes as well as for conferring solubility to misfolded proteins. To determine if O-mannosylation plays an essential role in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins, we used a model misfolded protein, Gas1*p. The O-mannose content of Gas1*p, which is transferred by protein O-mannosyltransferases, was higher than that of Gas1p. Both Pmt1p and Pmt2p, which do not transfer O-mannose to correctly folded Gas1p, participated in the O-mannosylation of Gas1*p. Furthermore, in a pmt1 Delta pmt2 Delta double-mutant background, degradation of Gas1*p is altered from a primarily proteasome dependent to a vacuolar protease-dependent pathway. This process is in a manner dependent on a Golgi-to-endosome sorting function of the VPS30 complex II. Collectively, our data suggest that O-mannosylation plays an important role for proteasome-dependent degradation of Gas1*p via the ERAD pathway and when O-mannosylation is insufficient, Gas1*p is degraded in the vacuole. Thus, we propose that O-mannosylation by Pmt1p and Pmt2p might be a key step in the targeting of some misfolded proteins for degradation via the proteasome-dependent ERAD pathway."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvm249"xsd:string
http://purl.uniprot.org/citations/18182384http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvm249"xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Fujita M."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Fujita M."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Hirayama H."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Hirayama H."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Jigami Y."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Jigami Y."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Yoko-o T."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/author"Yoko-o T."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/pages"555-567"xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/pages"555-567"xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/title"O-mannosylation is required for degradation of the endoplasmic reticulum-associated degradation substrate Gas1*p via the ubiquitin/proteasome pathway in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/title"O-mannosylation is required for degradation of the endoplasmic reticulum-associated degradation substrate Gas1*p via the ubiquitin/proteasome pathway in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/volume"143"xsd:string
http://purl.uniprot.org/citations/18182384http://purl.uniprot.org/core/volume"143"xsd:string
http://purl.uniprot.org/citations/18182384http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18182384
http://purl.uniprot.org/citations/18182384http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18182384