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http://purl.uniprot.org/citations/11914378http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11914378http://www.w3.org/2000/01/rdf-schema#comment"A critical step in S6 kinase 1 (S6K1) activation is Thr(229) phosphorylation in the activation loop by the phosphoinositide-dependent protein kinase (PDK1). Thr(229) phosphorylation requires prior phosphorylation of the Ser/Thr-Pro sites in the autoinhibitory domain and Thr(389) in the linker domain, consistent with PDK1 more effectively catalyzing Thr(229) phosphorylation in a variant harboring acidic residues in these positions (S6K1-E389D(3)E). S6K1-E389D(3)E has high basal activity and exhibits partial resistance to rapamycin and wortmannin, and its activity can be further augmented by mitogens, effects presumably mediated by Thr(229) phosphorylation. However, PDK1-induced Thr(229) phosphorylation is reported to be constitutive rather than phosphatidylinositide 3,4,5-trisphosphate-dependent, suggesting that S6K1-E389D(3)E activity is mediated through a distinct site. Here we use phosphospecific antibodies to show that Thr(229) is fully phosphorylated in S6K1-E389D(3)E in the absence of mitogens and that regulation of S6K1-E389D(3)E activity by mitogens, rapamycin, or wortmannin parallels Ser(371) phosphorylation. Consistent with this observation, a dominant interfering allele of the mammalian target of rapamycin, mTOR, inhibits mitogen-induced Ser(371) phosphorylation and activation of S6K1-E389D(3)E, whereas wild type mTOR stimulates both responses. Moreover, in vitro mTOR directly phosphorylates Ser(371), and this event modulates Thr(389) phosphorylation by mTOR, compatible with earlier in vivo findings."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201745200"xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/author"Thomas G."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/author"Brennan P."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/author"Saitoh M."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/author"Dennis P.B."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/author"Pullen N."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/author"Cantrell D."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/pages"20104-20112"xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/title"Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site."xsd:string
http://purl.uniprot.org/citations/11914378http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11914378http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11914378
http://purl.uniprot.org/citations/11914378http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11914378
http://purl.uniprot.org/uniprot/#_B7Z2K7-mappedCitation-11914378http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/#_Q15418-mappedCitation-11914378http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/#_Q63531-mappedCitation-11914378http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/#_P42346-mappedCitation-11914378http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/#_P23443-mappedCitation-11914378http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/P42346http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/B7Z2K7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/Q63531http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11914378
http://purl.uniprot.org/uniprot/P23443http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11914378