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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Matsumoto T,Yokote K,Take A,Takemoto M,Asaumi S,Hashimoto Y,Matsuda M,Saito Y,Mori Sdoi
10.1006/bbrc.2000.2374subject
Has Abstractpub_date
2000-04-02 00:00:00pages
28-33issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(00)92374-Xjournal_volume
270pub_type
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