Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl |
| |
Authors: | Grossmann A H Kolibaba K S Willis S G Corbin A S Langdon W S Deininger M W N Druker B J |
| |
Institution: | Department of Hematology & Medical Oncology, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, L592 Portland, OR 97239, USA. |
| |
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. |
| |
Keywords: | Protein tyrosine kinase Substrate specificity c-Cbl phosphorylation |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|