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Vol. 12, Issue 1, 1-12, January 2001
*Department of Microbiology, Health Sciences Center, University of
Virginia, Charlottesville, Virginia 22908 and §QCB, a
division of BioSource International, Hopkinton, Massachusetts 01748
Focal adhesion kinase (FAK) is an important regulator of
integrin signaling in adherent cells and accordingly its
activity is significantly modulated during mitosis when cells detach
from the extracellular matrix. During mitosis, FAK becomes heavily phosphorylated on serine residues concomitant with its inactivation and
dephosphorylation on tyrosine. Little is known about the regulation of
FAK activity by serine phosphorylation. In this report, we characterize
two novel sites of serine phosphorylation within the C-terminal domain
of FAK. Phosphorylation-specific antibodies directed to these sites and
against two previously characterized sites of serine phosphorylation
were used to study the regulated phosphorylation of FAK in
unsynchronized and mitotic cells. Among the four major phosphorylation
sites, designated pS1-pS4, phosphorylation of pS1 (Ser722) is unchanged
in unsynchronized and mitotic cells. In contrast, pS3 and pS4 (Ser843
and Ser910) exhibit increased phosphorylation during mitosis. In vitro
peptide binding experiments provide evidence that phosphorylation of
pS1 (Ser722) may play a role in modulating FAK binding to the SH3
domain of the adapter protein p130Cas.
Department of Genetics,
University of Pennsylvania, Philadelphia, PA 19104;
Janssen Pharmaceutica, Beerse, Belgium B-2340.
Corresponding author. E-mail address:
jtp{at}virginia.edu.
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