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Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation.

CrkII is an intracellular adaptor protein involved in signal transduction by various growth factors. Activation of PDGF alpha-receptor resulted in its association with CrkII in vivo. In contrast, binding of CrkII to the PDGF beta-receptor was negligible, despite its becoming prominently phosphorylated. Bacterially expressed GST-CrkII SH2 domain specifically bound to Tyr-762 and Tyr-771 in the activated PDGF alpha- and beta- receptors, respectively. GST fusion protein of full-length CrkII also bound to the activated PDGF beta-receptor. However, tyrosine phosphorylation of GST-CrkII diminished its binding to the beta-receptor. CrkI, a truncated version of CrkII lacking the phosphorylatable tyrosine residue, could bind to both PDGF alpha- and beta-receptors in vivo. In conclusion, tyrosine phosphorylation of CrkII negatively affects its binding to the PDGF receptors. The differential binding of CrkII to the PDGF alpha- and beta- receptors may be a rationale for functional diversity between the two receptors.

Pubmed ID: 10733900


  • Matsumoto T
  • Yokote K
  • Take A
  • Takemoto M
  • Asaumi S
  • Hashimoto Y
  • Matsuda M
  • Saito Y
  • Mori S


Biochemical and biophysical research communications

Publication Data

April 2, 2000

Associated Grants


Mesh Terms

  • Animals
  • Models, Biological
  • Phosphorylation
  • Platelet-Derived Growth Factor
  • Protein Binding
  • Protein Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-crk
  • Receptor, Platelet-Derived Growth Factor alpha
  • Receptor, Platelet-Derived Growth Factor beta
  • Recombinant Fusion Proteins
  • Signal Transduction
  • Swine
  • Tyrosine
  • src Homology Domains