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Article

Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor.

The Journal of biological chemistry - 27 Feb 2004

Ren Yuan, Meng Songshu, Mei Lin, Zhao Z Joe, Jove Richard, Wu Jie

Abstract excerpt

Epidermal growth factor (EGF) induces paxillin tyrosine dephosphorylation and Src activation, but the signaling pathways that mediate these responses were largely undefined. We found that Gab1, a docking protein for the SHP2 protein-tyrosine phosphatase in EGF-stimulated cells, was associated with paxillin. SHP2 dephosphorylated paxillin and caused dissociation of Csk, a negative regulator of Src, from paxillin...

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Share to CSK Tyrosine-Protein Kinase
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mitogen-Activated Protein Kinases

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Share to Protein Tyrosine Phosphatase, Non-Receptor Type 11

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Source

Identifiers

PMID: 14665621
DOI: 10.1074/jbc.M312575200

Genes

EGF

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.

Related research

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Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor.PMID 14665621Read ↗

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Development of an efficient "substrate-trapping" mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates.Semantic proximity Read ↗

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