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

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.

authors

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

doi

10.1006/bbrc.2000.2374

subject

Has Abstract

pub_date

2000-04-02 00:00:00

pages

28-33

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92374-X

journal_volume

270

pub_type

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