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Vol. 11, Issue 9, 3247-3263, September 2000
and
*Departments of Cell Biology & Anatomy, The carboxy-terminal 150 residues of the focal adhesion kinase
(FAK) comprise the focal adhesion-targeting sequence, which is
responsible for its subcellular localization. The mechanism of focal
adhesion targeting has not been fully elucidated. We describe a
mutational analysis of the focal adhesion-targeting sequence of FAK to
further examine the mechanism of focal adhesion targeting and explore
additional functions encoded by the carboxy-terminus of FAK. The
results demonstrate that paxillin binding is dispensable for focal
adhesion targeting of FAK. Cell adhesion-dependent tyrosine phosphorylation strictly correlated with the ability of mutants to
target to focal adhesions. Focal adhesion targeting was also a
requirement for maximal FAK-dependent tyrosine phosphorylation of
paxillin and FAK-related nonkinase (FRNK)-dependent inhibition of
endogenous FAK function. However, there were additional requirements for these latter functions because we identified mutants that target to
focal adhesions, yet are defective for the induction of paxillin
phosphorylation or the dominant-negative function of FRNK. Furthermore,
the paxillin-binding activity of FRNK mutants did not correlate with
their ability to inhibit FAK, suggesting that FRNK has other targets in
addition to paxillin.
Pediatrics,
and Anesthesiology, and §Lineberger
Comprehensive Cancer Center, University of North Carolina, Chapel Hill,
North Carolina 27599
Corresponding author: E-mail address:
crispy4{at}med.unc.edu.
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