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Biochem Biophys Res Commun. 2000 Apr 2;270(1):28-33.

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

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  • 1Second Department of Internal Medicine, Chiba University School of Medicine, 1-8-1 Inohana, Chuo-ku, Chiba, 260-0856, Japan.

Abstract

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.

Copyright 2000 Academic Press.

PMID:
10733900
[PubMed - indexed for MEDLINE]
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