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The Focal Adhesion Kinase‐‐A Regulator of Cell Migration and Invasion
Author(s) -
Hauck Christof R.,
Hsia Datsun A.,
Schlaepfer David D.
Publication year - 2002
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540211470
Subject(s) - focal adhesion , microbiology and biotechnology , ptk2 , cell migration , integrin , extracellular matrix , biology , signal transduction , cell adhesion , tyrosine kinase , kinase , cancer research , protein kinase a , cell , mitogen activated protein kinase kinase , biochemistry
Cell migration plays an important role in embryonic development, wound healing, immune responses, and in pathological phenomena such as tissue invasion and metastasis formation. In this review, we summarize recent reports that connect the focal adhesion kinase (FAK) to cell migration and invasion. FAK is a nonreceptor protein tyrosine kinase involved in signal transduction from integrin‐enriched focal adhesion sites that mediate cell contact with the extracellular matrix. Multiple protein‐protein interaction sites allow FAK to associate with adapter and structural proteins allowing for the modulation of mitogen‐activated protein (MAP) kinases, stress‐activated protein (SAP) kinases, and small GTPase activity. FAK‐enhanced signals have been shown to mediate the survival of anchorage‐dependent cells and are critical for efficient cell migration in response to growth factor receptor and integrin stimulation. Elevated expression of FAK in human tumors has been correlated with increased malignancy and invasiveness. Because recent findings show that FAK contributes to the secretion of matrix‐metalloproteinases, FAK may represent an important checkpoint in coordinating the dynamic processes of cell motility and extracellular matrix remodeling during tumor cell invasion.