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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RA7I0tLuqe6iMZOjGtza0Uuk5LbomqYDpQg5xbjidOLwc#_6 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RA7I0tLuqe6iMZOjGtza0Uuk5LbomqYDpQg5xbjidOLwc#_5 http://www.w3.org/ns/prov#value FAK may be recruited to nascent focal adhesions because it interacts, either directly or through the cytoskeletal proteins talin and paxillin, with the cytoplasmic tail of integrin b subunits (8). Upon activation, FAK autophosphorylates Tyr397, creating a binding site for the Src homology 2 (SH2) domain of Src or Fyn (9, 10). The Src kinase then phosphorylates a number of focal adhesion components. 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