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http://purl.uniprot.org/citations/22009749http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22009749http://www.w3.org/2000/01/rdf-schema#comment"Phosphatases of the regenerating liver (PRL) play oncogenic roles in cancer development and metastasis. Although previous studies indicate that PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways, the mechanism by which it activates these signaling events remains unclear. We have identified a PRL-1-binding peptide (Peptide 1) that shares high sequence identity with a conserved motif in the Src homology 3 (SH3) domain of p115 Rho GTPase-activating protein (GAP). p115 RhoGAP directly binds PRL-1 in vitro and in cells via its SH3 domain. Structural analyses of the PRL-1·Peptide 1 complex revealed a novel protein-protein interaction whereby a sequence motif within the PxxP ligand-binding site of the p115 RhoGAP SH3 domain occupies a folded groove within PRL-1. This prevents the canonical interaction between the SH3 domain of p115 RhoGAP and MEKK1 and results in activation of ERK1/2. Furthermore, PRL-1 binding activates RhoA signaling by inhibiting the catalytic activity of p115 RhoGAP. The results demonstrate that PRL-1 binding to p115 RhoGAP provides a coordinated mechanism underlying ERK1/2 and RhoA activation."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.286302"xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Bai Y."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Cao Y."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Dong Y."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Luo Y."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Liu S."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Zhang L."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Shen K."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Zhang Z.Y."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Wells C.D."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Quilliam L.A."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/author"Walls C.D."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/pages"42316-42324"xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/title"PRL-1 protein promotes ERK1/2 and RhoA protein activation through a non-canonical interaction with the Src homology 3 domain of p115 Rho GTPase-activating protein."xsd:string
http://purl.uniprot.org/citations/22009749http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/22009749http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22009749
http://purl.uniprot.org/citations/22009749http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22009749
http://purl.uniprot.org/uniprot/#_A0A024R324-mappedCitation-22009749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22009749
http://purl.uniprot.org/uniprot/#_P61586-mappedCitation-22009749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22009749
http://purl.uniprot.org/uniprot/#_P63085-mappedCitation-22009749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22009749
http://purl.uniprot.org/uniprot/#_A0A0B4J1X7-mappedCitation-22009749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22009749