Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl

A. H. Grossmann, K. S. Kolibaba, S. G. Willis, A. S. Corbin, W. S. Langdon, M. W.N. Deininger, B. J. Druker

Research output: Contribution to journalArticle

13 Scopus citations

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 languageEnglish (US)
Pages (from-to)555-562
Number of pages8
JournalFEBS Letters
Volume577
Issue number3
DOIs
StatePublished - 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

Fingerprint Dive into the research topics of 'Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl'. Together they form a unique fingerprint.

  • Cite this

    Grossmann, A. H., Kolibaba, K. S., Willis, S. G., Corbin, A. S., Langdon, W. S., Deininger, M. W. N., & Druker, B. J. (2004). Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl. FEBS Letters, 577(3), 555-562. https://doi.org/10.1016/j.febslet.2004.10.054