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Signaling through focal adhesion kinase
Author(s) -
Hanks Steven K.,
Polte Thomas R.
Publication year - 1997
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950190208
Subject(s) - ptk2 , focal adhesion , paxillin , proto oncogene tyrosine protein kinase src , microbiology and biotechnology , integrin , adapter molecule crk , tyrosine phosphorylation , cell adhesion , sh3 domain , tyrosine kinase , biology , actin cytoskeleton , signal transduction , cytoskeleton , signal transducing adaptor protein , cell , protein kinase c , biochemistry , mitogen activated protein kinase kinase
Focal adhesion kinase (FAK) is a nonreceptor protein‐tyrosine kinase implicated in controlling cellular responses to the engagement of cell‐surface integrins, including cell spreading and migration, survival and proliferation. Aberrant FAK signaling may contribute to the process of cell transformation by certain oncoproteins, including v‐Src. Progress toward elucidating the events leading to FAK activation following integrin‐mediated cell adhesion, as well as events downstream of FAK, has come through the identification of FAK phosphorylation sites and interacting proteins. A signaling partnership is formed between FAK and Src‐family kinases, leading to tyrosine phosphorylation of FAK and associated ‘docking’ proteins Cas and paxillin. Subsequent recruitment of proteins containing Src homology 2 domains, including Grb2 and c‐Crk, to the complex is likely to trigger adhesion‐induced cellular responses, including changes to the actin cytoskeleton and activation of the Ras‐MAP kinase pathway.