A new method for isolating tyrosine kinase substrates used to identify Fish, an SH3 and PX domain-containing protein, and Src substrate
Copyright policy )A new method for isolating tyrosine kinase substrates used to identify Fish, an SH3 and PX domain-containing protein, and Src substrate
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.
- Ludwig Cancer Research Australia
- European Molecular Biology Laboratory Germany
- Ludwig Cancer Research Belgium
Molecular Sequence Data, 3T3 Cells, Phosphate-Binding Proteins, Protein-Tyrosine Kinases, Phosphoproteins, Substrate Specificity, src Homology Domains, Mice, Organ Specificity, Animals, Amino Acid Sequence, RNA, Messenger, Phosphorylation, Phosphotyrosine
Molecular Sequence Data, 3T3 Cells, Phosphate-Binding Proteins, Protein-Tyrosine Kinases, Phosphoproteins, Substrate Specificity, src Homology Domains, Mice, Organ Specificity, Animals, Amino Acid Sequence, RNA, Messenger, Phosphorylation, Phosphotyrosine
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