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http://purl.uniprot.org/citations/19026786http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19026786http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19026786http://www.w3.org/2000/01/rdf-schema#comment"PH domains, by binding to phosphoinositides, often serve as membrane-targeting modules. Using crystallographic, biochemical, and cell biological approaches, we have uncovered a mechanism that the integrin-signaling adaptor Skap-hom uses to mediate cytoskeletal interactions. Skap-hom is a homodimer containing an N-terminal four-helix bundle dimerization domain, against which its two PH domains pack in a conformation incompatible with phosphoinositide binding. The isolated PH domains bind PI[3,4,5]P(3), and mutations targeting the dimerization domain or the PH domain's PI[3,4,5]P(3)-binding pocket prevent Skap-hom localization to ruffles. Targeting is retained when the PH domain is deleted or by combined mutation of the PI[3,4,5]P(3)-binding pocket and the PH/dimerization domain interface. Thus, the dimerization and PH domain form a PI[3,4,5]P(3)-responsive molecular switch that controls Skap-hom function."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2008.09.022"xsd:string
http://purl.uniprot.org/citations/19026786http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2008.09.022"xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Ceccarelli D.F."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Ceccarelli D.F."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Eck M.J."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Eck M.J."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Tang Y."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Tang Y."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Swanson K.D."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Swanson K.D."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Poy F."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Poy F."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Neel B.G."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Neel B.G."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Sliwa J.P."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/author"Sliwa J.P."xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/pages"564-575"xsd:string
http://purl.uniprot.org/citations/19026786http://purl.uniprot.org/core/pages"564-575"xsd:string