Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl.
Catalytic (SH1) domains of protein tyrosine kinases (PTKs) demonstrate specificity for peptide substrates. Whether SH1 domains differentiate between tyrosines in a physiological substrate has not been confirmed. Using purified proteins, we studied the ability of Syk, Fyn, and Abl to differentiate between tyrosines in a common PTK substrate, c-Cbl. We ... found that each kinase produced a distinct pattern of c-Cbl phosphorylation, which altered the phosphotyrosine-dependent interactions between c-Cbl and CrkL or phosphatidylinositol 3'-kinase (PI3-K). Our data support the concept that SH1 domains determine the final sites of phosphorylation once PTKs reach their target proteins.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Catalytic Domain, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Glutathione Transferase, Immunoblotting, Phosphorylation, Plasmids, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Recombinant Fusion Proteins, Substrate Specificity, Tyrosine, Ubiquitin-Protein Ligases, src Homology Domains
Amino Acid Sequence, Binding Sites, Catalytic Domain, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Glutathione Transferase, Immunoblotting, Phosphorylation, Plasmids, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Recombinant Fusion Proteins, Substrate Specificity, Tyrosine, Ubiquitin-Protein Ligases, src Homology Domains
FEBS Lett.
Date: Nov. 19, 2004
PubMed ID: 15556646
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