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http://purl.uniprot.org/citations/23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23386617http://www.w3.org/2000/01/rdf-schema#comment"RGC1 and RGC2 comprise a functional RalGAP complex (RGC) that suppresses RalA activity. The PI3-kinase/Akt signaling pathway activates RalA through phosphorylation-mediated inhibition of the RGC. Here we identify a novel phosphorylation-dependent interaction between 14-3-3 and the RGC. 14-3-3 binds to the complex through an Akt-phosphorylated residue, threonine 715, on RGC2. Interaction with 14-3-3 does not alter in vitro activity of the GTPase-activating protein complex. However, blocking the interaction between 14-3-3 and RGC2 in cells increases suppression of RalA activity by the RGC, suggesting that 14-3-3 inhibits the complex through a non-catalytic mechanism. Together, these data show that 14-3-3 negatively regulates the RGC downstream of the PI3-kinase/Akt signaling pathway."xsd:string
http://purl.uniprot.org/citations/23386617http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m112.426106"xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/author"Saltiel A.R."xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/author"Chen X.W."xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/author"Williams A."xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/author"Uhm M."xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/author"Leto D."xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/pages"9272-9283"xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/title"Negative regulation of the RalGAP complex by 14-3-3."xsd:string
http://purl.uniprot.org/citations/23386617http://purl.uniprot.org/core/volume"288"xsd:string
http://purl.uniprot.org/citations/23386617http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23386617
http://purl.uniprot.org/citations/23386617http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23386617
http://purl.uniprot.org/uniprot/#_E2I6G1-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_D3YY41-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_B3KVH4-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_A0A0S2Z3D6-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_A0A2P0XI22-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_A0A3G2C3N5-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_A0A8A2FPJ2-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_A3KMH3-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_A0A142IKA9-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617
http://purl.uniprot.org/uniprot/#_B0LPE5-mappedCitation-23386617http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23386617