Abstract
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.
Original language | English (US) |
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Pages (from-to) | 555-562 |
Number of pages | 8 |
Journal | FEBS Letters |
Volume | 577 |
Issue number | 3 |
DOIs | |
State | Published - Nov 19 2004 |
Keywords
- Protein tyrosine kinase
- Substrate specificity
- c-Cbl phosphorylation
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology