Review
doi: 10.1002/(SICI)1521-1878(199912)22:1<1069::AID-BIES13>3.0.CO;2-C.
Why do so many stimuli induce tyrosine phosphorylation of FAK?
Affiliations
- PMID: 10580994
- DOI: 10.1002/(SICI)1521-1878(199912)22:1<1069::AID-BIES13>3.0.CO;2-C
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Review
Why do so many stimuli induce tyrosine phosphorylation of FAK?
Bioessays.
1999 Dec.
Abstract
Engagement of integrins and other adhesion receptors can induce tyrosine phosphorylation of focal adhesion kinase (FAK), a tyrosine kinase present in focal adhesions. Furthermore, in addition to adhesion receptors, a surprising variety of stimuli, acting either on specific surface receptors or on intracellular molecules, such as PKC or Rho, can induce also tyrosine phosphorylation of FAK. I suggest that a potential mechanism by which such distinct factors may modulate the tyrosine phosphorylation of FAK is the promotion of integrin or other adhesion receptor clustering at focal adhesions.
Copyright 1999 John Wiley & Sons, Inc.
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