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http://purl.uniprot.org/citations/18285345http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18285345http://www.w3.org/2000/01/rdf-schema#comment"The activation of the protein kinase C (PKC) family of serine/threonine kinases contributes to the modulation of insulin signaling, and the PKC-dependent phosphorylation of insulin receptor substrate (IRS)-1 has been implicated in the development of insulin resistance. Here we demonstrate Ser(357) of rat IRS-1 as a novel PKC-delta-dependent phosphorylation site in skeletal muscle cells upon stimulation with insulin and phorbol ester using Ser(P)(357) antibodies and active and kinase dead mutants of PKC-delta. Phosphorylation of this site was simulated using IRS-1 Glu(357) and shown to reduce insulin-induced tyrosine phosphorylation of IRS-1, to decrease activation of Akt, and to subsequently diminish phosphorylation of glycogen synthase kinase-3. When the phosphorylation was prevented by mutation of Ser(357) to alanine, these effects of insulin were enhanced. When the adjacent Ser(358), present in mouse and rat IRS-1, was mutated to alanine, which is homologous to the human sequence, the insulin-induced phosphorylation of glycogen synthase kinase-3 or tyrosine phosphorylation of IRS-1 was not increased. Moreover, both active PKC-delta and phosphorylation of Ser(357) were shown to be necessary for the attenuation of insulin-stimulated Akt phosphorylation. The phosphorylation of Ser(357) could lead to increased association of PKC-delta to IRS-1 upon insulin stimulation, which was demonstrated with IRS-1 Glu(357). Together, these data suggest that phosphorylation of Ser(357) mediates at least in part the adverse effects of PKC-delta activation on insulin action."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m708588200"xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Lehmann R."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Voelter W."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Kalbacher H."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Haring H.U."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Schleicher E.D."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Hennige A.M."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Weigert C."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Lutz S.Z."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/author"Waraich R.S."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/pages"11226-11233"xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/title"Phosphorylation of Ser357 of rat insulin receptor substrate-1 mediates adverse effects of protein kinase C-delta on insulin action in skeletal muscle cells."xsd:string
http://purl.uniprot.org/citations/18285345http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18285345http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18285345
http://purl.uniprot.org/citations/18285345http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18285345
http://purl.uniprot.org/uniprot/P49840#attribution-B4E82EFE2857CBEA2D6D16A36D692F21http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18285345
http://purl.uniprot.org/uniprot/Q2NL51#attribution-D8920BCE066E40E8CE99C5A390C1F623http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18285345
http://purl.uniprot.org/uniprot/P28867#attribution-051F9EA69CD26504785D74B143017E61http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18285345
http://purl.uniprot.org/uniprot/P28867#attribution-A3BA8228C6A07BFF3FDF4DEC65431805http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18285345
http://purl.uniprot.org/uniprot/P35570#attribution-051F9EA69CD26504785D74B143017E61http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18285345
http://purl.uniprot.org/uniprot/P35570#attribution-A3BA8228C6A07BFF3FDF4DEC65431805http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18285345