Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 334, Issue 4, Pages 1299-1304Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2005.07.034
Keywords
integrin; fibronectin; auto-inhibition; autophosphorylation; focal adhesions; focal adhesion kinase; FAK Tyr-397; cell adhesion; cell suspension; FAK -/- cells
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Funding
- NIDDK NIH HHS [DK 55003, DK 56930] Funding Source: Medline
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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 (FAK Delta 384). FAK Delta 384 showed a striking increase in phosphorylation, as compared with wild type FAK, in lysates of either HEK293 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. (c) 2005 Elsevier Inc. All rights reserved.
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