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Article

Residues within the first subdomain of the FERM-like domain in focal adhesion kinase are important in its regulation.

The Journal of biological chemistry - 4 Mar 2005

Cohen Lee Ann, Guan Jun-Lin

Abstract excerpt

We have previously described regulation of focal adhesion kinase (FAK) by its amino-terminal FERM-like domain through an autoinhibitory interaction with its kinase domain (Cooper, L. A., Shen, T. L., and Guan, J. L. (2003) Mol. Cell. Biol. 23, 8030-8041). Here we show that the first two subdomains of the FERM-like domain are independently capable of inhibiting phosphorylation of FAK in trans. We characterized...

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Identifiers

PMID: 15611137
DOI: 10.1074/jbc.M412021200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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