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Article

Complex formation with focal adhesion kinase: A mechanism to regulate activity and subcellular localization of Src kinases.

Molecular biology of the cell - 1 Oct 1999

Schaller M D, Hildebrand J D, Parsons J T

Abstract excerpt

Tyrosine phosphorylation of focal adhesion kinase (FAK) creates a high-affinity binding site for the src homology 2 domain of the Src family of tyrosine kinases. Assembly of a complex between FAK and Src kinases may serve to regulate the subcellular localization and the enzymatic activity of members of the Src family of kinases. We show that simultaneous overexpression of FAK and pp60(c-src) or p59(fyn) results...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 10512882
DOI: 10.1091/mbc.10.10.3489
PMCID: PMC25619

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Complex formation with focal adhesion kinase: A mechanism to regulate activity and subcellular localization of Src kinases.PMID 10512882Read ↗

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