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http://purl.uniprot.org/citations/31663027http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31663027http://www.w3.org/2000/01/rdf-schema#comment"PIP3-dependent Rac exchanger 1 (P-Rex1) is activated downstream of G protein-coupled receptors to promote neutrophil migration and metastasis. The structure of more than half of the enzyme and its regulatory G protein binding site are unknown. Our 3.2 Å cryo-EM structure of the P-Rex1-Gβγ complex reveals that the carboxyl-terminal half of P-Rex1 adopts a complex fold most similar to those of Legionella phosphoinositide phosphatases. Although catalytically inert, the domain coalesces with a DEP domain and two PDZ domains to form an extensive docking site for Gβγ. Hydrogen-deuterium exchange mass spectrometry suggests that Gβγ binding induces allosteric changes in P-Rex1, but functional assays indicate that membrane localization is also required for full activation. Thus, a multidomain assembly is key to the regulation of P-Rex1 by Gβγ and the formation of a membrane-localized scaffold optimized for recruitment of other signaling proteins such as PKA and PTEN."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.aax8855"xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Gutkind J.S."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Tesmer J.J.G."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Urata S."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Ravala S.K."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Cianfrocco M.A."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Cash J.N."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Avramova L.V."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/author"Shost M.D."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/name"Sci Adv"xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/pages"eaax8855"xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/title"Cryo-electron microscopy structure and analysis of the P-Rex1-Gbetagamma signaling scaffold."xsd:string
http://purl.uniprot.org/citations/31663027http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/31663027http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31663027
http://purl.uniprot.org/citations/31663027http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31663027
http://purl.uniprot.org/uniprot/#_A0A2X0SFH1-mappedCitation-31663027http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31663027
http://purl.uniprot.org/uniprot/#_P62871-mappedCitation-31663027http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31663027
http://purl.uniprot.org/uniprot/#_P63212-mappedCitation-31663027http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31663027
http://purl.uniprot.org/uniprot/#_Q8TCU6-mappedCitation-31663027http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31663027
http://purl.uniprot.org/uniprot/P62871http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31663027
http://purl.uniprot.org/uniprot/A0A2X0SFH1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31663027