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http://purl.uniprot.org/citations/17115053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17115053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17115053http://www.w3.org/2000/01/rdf-schema#comment"Although diverse signaling cascades require the coordinated regulation of heterotrimeric G proteins and small GTPases, these connections remain poorly understood. We present the crystal structure of the GTPase Rac1 bound to phospholipase C-beta2 (PLC-beta2), a classic effector of heterotrimeric G proteins. Rac1 engages the pleckstrin-homology (PH) domain of PLC-beta2 to optimize its orientation for substrate membranes. Gbetagamma also engages the PH domain to activate PLC-beta2, and these two activation events are compatible, leading to additive stimulation of phospholipase activity. In contrast to PLC-delta, the PH domain of PLC-beta2 cannot bind phosphoinositides, eliminating this mode of regulation. The structure of the Rac1-PLC-beta2 complex reveals determinants that dictate selectivity of PLC-beta isozymes for Rac GTPases over other Rho-family GTPases, and substitutions within PLC-beta2 abrogate its stimulation by Rac1 but not by Gbetagamma, allowing for functional dissection of this integral signaling node."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1175"xsd:string
http://purl.uniprot.org/citations/17115053http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1175"xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Sondek J."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Sondek J."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Harden T.K."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Harden T.K."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Worthylake D.K."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Worthylake D.K."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Jezyk M.R."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Jezyk M.R."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Snyder J.T."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Snyder J.T."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Gershberg S."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/author"Gershberg S."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/pages"1135-1140"xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/pages"1135-1140"xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/title"Crystal structure of Rac1 bound to its effector phospholipase C-beta2."xsd:string
http://purl.uniprot.org/citations/17115053http://purl.uniprot.org/core/title"Crystal structure of Rac1 bound to its effector phospholipase C-beta2."xsd:string