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http://purl.uniprot.org/citations/10805787http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10805787http://www.w3.org/2000/01/rdf-schema#comment"STATs are activated by tyrosine phosphorylation on cytokine stimulation. A tyrosine-phosphorylated STAT forms a functional dimer through reciprocal Src homology 2 domain (SH2)-phosphotyrosyl peptide interactions. IFN treatment induces the association of PIAS1 and Stat1, which results in the inhibition of Stat1-mediated gene activation. The molecular basis of the cytokine-dependent PIAS1-Stat1 interaction has not been understood. We report here that a region near the COOH terminus of PIAS1 (amino acids 392-541) directly interacts with the NH(2)-terminal domain of Stat1 (amino acids 1-191). A mutant PIAS1 lacking the Stat1-interacting domain failed to inhibit Stat1-mediated gene activation. By using a modified yeast two-hybrid assay, we demonstrated that PIAS1 specifically interacts with the Stat1 dimer, but not tyrosine-phosphorylated or -unphosphorylated Stat1 monomer. In addition, whereas the NH(2)-terminal region of PIAS1 does not interact with Stat1, it serves as a modulatory domain by preventing the interaction of the COOH-terminal domain of PIAS1 with the Stat1 monomer. Thus, the cytokine-induced PIAS1-Stat1 interaction is mediated through the specific recognition of the dimeric form of Stat1 by PIAS1."xsd:string
http://purl.uniprot.org/citations/10805787http://purl.org/dc/terms/identifier"doi:10.1073/pnas.97.10.5267"xsd:string
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/author"Fu Y."xsd:string
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/author"Liao J."xsd:string
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/author"Shuai K."xsd:string
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/pages"5267-5272"xsd:string
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/title"Distinct roles of the NH2- and COOH-terminal domains of the protein inhibitor of activated signal transducer and activator of transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1-Stat1 interaction."xsd:string
http://purl.uniprot.org/citations/10805787http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/10805787http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10805787
http://purl.uniprot.org/citations/10805787http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10805787
http://purl.uniprot.org/uniprot/O75925#attribution-2E82831C49426E880BD2895E1743C111http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10805787
http://purl.uniprot.org/uniprot/#_P42224-mappedCitation-10805787http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10805787
http://purl.uniprot.org/uniprot/#_O75925-mappedCitation-10805787http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10805787
http://purl.uniprot.org/uniprot/#_P63165-mappedCitation-10805787http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10805787
http://purl.uniprot.org/uniprot/P63165http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10805787
http://purl.uniprot.org/uniprot/P42224http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10805787
http://purl.uniprot.org/uniprot/O75925http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10805787