Year: 2004
Type: article
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.
Source: FEBS Letters
Authors: A.H. Grossmann, K.S. Kolibaba, S.G. Willis, A.S. Corbin, W.S. Langdon, M.W.N. Deininger, B.J. Druker
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Award: G2600633667
OpenAlex ID: W2115404455
