Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 24, Issue 12, Pages 5353-5368Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.24.12.5353-5368.2004
Keywords
-
Categories
Funding
- NCI NIH HHS [P30 CA016086, CA90901, R01 CA090901] Funding Source: Medline
Ask authors/readers for more resources
From the results of deletion analyses, the FERM domain of FAK has been proposed to inhibit enzymatic activity and repress FAK signaling. We have identified a sequence in the FERM domain that is important for FAK signaling in vivo. Point mutations in this sequence had little effect upon catalytic activity in vitro. However, the mutant exhibits reduced tyrosine phosphorylation and dramatically reduced Src family kinase binding. Further, the abilities of the mutant to transduce biochemical signals and to promote cell migration were severely impaired. The results implicate a FERM domain interaction in cell adhesion-dependent activation of FAK and downstream signaling. We also show that the purified FERM domain of FAK interacts with full-length FAK in vitro, and mutation of this sequence disrupts the interaction. These findings are discussed in the context of models of FAK regulation by its FERM domain.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available