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Article

Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK.

The Journal of experimental medicine - 1 Oct 1995

Tachibana K, Sato T, D'Avirro N, Morimoto C

Abstract excerpt

Focal adhesion kinase (pp125FAK) is localized to focal adhesions and tyrosine phosphorylated by the engagement of beta 1 integrins. However, it is unclear how pp125FAK is linked to integrin molecules. We demonstrate that pp125FAK is directly associated with paxillin, a 68-kD cytoskeleton protein. The COOH-terminal domain of pp125FAK spanning FAK residues 919-1042 is sufficient for paxillin binding and has...

Topics

Amino Acid Sequence
Animals
Binding Sites
Cell Adhesion Molecules
Cloning, Molecular
Cytoskeletal Proteins
Fluorescent Antibody Technique
Focal Adhesion Kinase 1
Focal Adhesion Protein-Tyrosine Kinases
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Immunoblotting

Mice

Molecular Sequence Data

Mutation

Paxillin

Phosphoproteins

Precipitin Tests

Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 7561682
DOI: 10.1084/jem.182.4.1089
PMCID: PMC2192281

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7561682-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK.PMID 7561682Read ↗

Focal adhesion targeting: the critical determinant of FAK regulation and substrate phosphorylation.Semantic proximity Read ↗

Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation.Semantic proximity Read ↗

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Modulation of cell spreading and migration by pp125FAK phosphorylation.Semantic proximity Read ↗

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