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Biochem Biophys Res Commun. 2005 Sep 9;334(4):1299-304.

A truncated FAK lacking the FERM domain displays high catalytic activity but retains responsiveness to adhesion-mediated signals.

Author information

1
Division of Digestive Diseases, Department of Medicine, David Geffen School of Medicine, CURE: Digestive Diseases Research Center, Molecular Biology Institute, University of California at Los Angeles, USA.

Abstract

In order to determine the role of the FERM domain in the regulation of FAK phosphorylation at Tyr-397, the major autophosphorylation site, we generated a truncated FAK lacking a region of the N-terminus corresponding to amino acids 1-384 (FAKDelta384). FAKDelta384 showed a striking increase in phosphorylation, as compared with wild type FAK, in lysates of either HEK 293 or FAK-/- cells. Interestingly, the truncated form of FAK lacking the N-terminal domain retains responsiveness to integrin-mediated signals, as judged by its dephosphorylation by holding cells in suspension and by the recovery of the phosphorylation when replating the cells on fibronectin. We propose a model in which removal of FERM-mediated auto-inhibition is important to increase FAK catalytic activity but the translocation and clustering of this enzyme at the focal adhesions is required for maximal phosphorylation at Tyr-397.

PMID:
16039608
DOI:
10.1016/j.bbrc.2005.07.034
[Indexed for MEDLINE]

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