A new method for isolating tyrosine kinase substrates used to identify Fish, an SH3 and PX domain-containing protein, and Src substrate

Peter Lock, Clare L. Abram, Toby Gibson, Sara A. Courtneidge

Research output: Contribution to journalArticle

138 Scopus citations


We describe a method for identifying tyrosine kinase substrates using anti-phosphotyrosine antibodies to screen tyrosine-phosphorylated cDNA expression libraries. Several potential Src substrates were identified including Fish, which has five SH3 domains and a recently discovered phox homology (PX) domain. Fish is tyrosine-phosphorylated in Src-transformed fibroblasts (suggesting that it is a target of Src in vivo) and in normal cells following treatment with several growth factors. Treatment of cells with cytochalasin D also resulted in rapid tyrosine phosphorylation of Fish, concomitant with activation of Src. These data suggest that Fish is involved in signalling by tyrosine kinases, and imply a specialized role in the actin cytoskeleton.

Original languageEnglish (US)
Pages (from-to)4346-4357
Number of pages12
JournalEMBO Journal
Issue number15
StatePublished - Aug 3 1998



  • Cytochalasin D
  • Fish
  • PX domain
  • Src
  • Tyrosine kinase substrate

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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