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http://purl.uniprot.org/citations/30611118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30611118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30611118http://www.w3.org/2000/01/rdf-schema#comment"The second messenger 3',5'-cyclic adenosine monophosphate (cAMP) stimulates gene expression via the cAMP-regulated transcriptional coactivator (CRTC) family of cAMP response element-binding protein coactivators. In the basal state, CRTCs are phosphorylated by salt-inducible kinases (SIKs) and sequestered in the cytoplasm by 14-3-3 proteins. cAMP signaling inhibits the SIKs, leading to CRTC dephosphorylation and nuclear translocation. Here we show that although all CRTCs are regulated by SIKs, their interactions with Ser/Thr-specific protein phosphatases are distinct. CRTC1 and CRTC2 associate selectively with the calcium-dependent phosphatase calcineurin, whereas CRTC3 interacts with B55 PP2A holoenzymes via a conserved PP2A-binding region (amino acids 380-401). CRTC3-PP2A complex formation was induced by phosphorylation of CRTC3 at S391, facilitating the subsequent activation of CRTC3 by dephosphorylation at 14-3-3 binding sites. As stimulation of mitogenic pathways promoted S391 phosphorylation via the activation of ERKs and CDKs, our results demonstrate how a ubiquitous phosphatase enables cross talk between growth factor and cAMP signaling pathways at the level of a transcriptional coactivator."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.org/dc/terms/identifier"doi:10.1016/j.isci.2018.12.012"xsd:string
http://purl.uniprot.org/citations/30611118http://purl.org/dc/terms/identifier"doi:10.1016/j.isci.2018.12.012"xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Montminy M."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Montminy M."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Moresco J.J."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Moresco J.J."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Ostojic J."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Ostojic J."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Sonntag T."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Sonntag T."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Yates J.R. III"xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Yates J.R. III"xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Vaughan J.M."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Vaughan J.M."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Yoon Y.S."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/author"Yoon Y.S."xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/name"IScience"xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/name"IScience"xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/pages"134-145"xsd:string
http://purl.uniprot.org/citations/30611118http://purl.uniprot.org/core/pages"134-145"xsd:string