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J Biol Chem, Vol. 274, Issue 38, 26901-26906, September 17, 1999
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From the Focal adhesion kinase (FAK) has been implicated
to play a role in suppression of apoptosis. In this study, we have
demonstrated that UV irradiation induced cleavage of FAK and two of its
interacting proteins Src and p130Cas in Madin-Darby
canine kidney cells, concomitant with an increase in cell death. The
cleavage of these proteins upon UV irradiation was completely inhibited
by ZVAD-FMK, a broad range inhibitor of caspases, and apparently
delayed by Bcl2 overexpression. To examine if FAK plays a role in
suppressing UV-induced apoptosis, stable Madin-Darby canine kidney cell
lines overexpressing FAK were established. Our results showed that a
marked (30-40%) increase in cell survival upon UV irradiation was
achieved by this strategy. In our efforts to determine the mechanism by
which FAK transduces survival signals to the downstream, we found that
a FAK mutant deficient in binding to phosphatidylinositol 3-kinase
failed to promote cell survival. Moreover, the expression of the Src
homology 3 domain of p130Cas, which competed with
endogenous p130Cas for FAK binding, abrogated the
FAK-promoted cell survival. Together, these results suggest that the
integrity of FAK and its binding to phosphatidylinositol 3-kinase and
p130Cas are required for FAK to exert its antiapoptotic function.
Department of Zoology and the
Institute of Biochemistry, National Chung Hsing
University, Taichung, Taiwan, Republic of China, the
§ Section of Nephrology, Taichung Veterans General Hospital,
Taichung, Taiwan, Republic of China, and the ¶ Department of
Physiology, National Cheng Kung University Medical College,
Tainan, Taiwan, Republic of China
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