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http://purl.uniprot.org/citations/24480479http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24480479http://www.w3.org/2000/01/rdf-schema#comment"Focal adhesion kinase (FAK) controls adhesion-dependent cell motility, survival, and proliferation. FAK has kinase-dependent and kinase-independent functions, both of which play major roles in embryogenesis and tumor invasiveness. The precise mechanisms of FAK activation are not known. Using x-ray crystallography, small angle x-ray scattering, and biochemical and functional analyses, we show that the key step for activation of FAK's kinase-dependent functions--autophosphorylation of tyrosine-397--requires site-specific dimerization of FAK. The dimers form via the association of the N-terminal FERM domain of FAK and are stabilized by an interaction between FERM and the C-terminal FAT domain. FAT binds to a basic motif on FERM that regulates co-activation and nuclear localization. FAK dimerization requires local enrichment, which occurs specifically at focal adhesions. Paxillin plays a dual role, by recruiting FAK to focal adhesions and by reinforcing the FAT:FERM interaction. Our results provide a structural and mechanistic framework to explain how FAK combines multiple stimuli into a site-specific function. The dimer interfaces we describe are promising targets for blocking FAK activation."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.org/dc/terms/identifier"doi:10.1002/embj.201386399"xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Ortega A."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Walkiewicz K."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Boutterin M.C."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Arold S.T."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Girault J.A."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Gasmi L."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Arsenieva D."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Leonard P.G."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Bouceba T."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Kadare G."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Gervasi N."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Brami-Cherrier K."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/author"Seantier B."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/pages"356-370"xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/title"FAK dimerization controls its kinase-dependent functions at focal adhesions."xsd:string
http://purl.uniprot.org/citations/24480479http://purl.uniprot.org/core/volume"33"xsd:string
http://purl.uniprot.org/citations/24480479http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24480479
http://purl.uniprot.org/citations/24480479http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24480479
http://purl.uniprot.org/uniprot/O35346#attribution-F0A489567E8F46C3F324FDCB8B5DF3E0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24480479
http://purl.uniprot.org/uniprot/#_A0A0G2KAT5-mappedCitation-24480479http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24480479