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Distinct regions of the granulocyte colony-stimulating factor receptor are
required for tyrosine phosphorylation of the signaling molecules JAK2,
Stat3, and p42, p44MAPK
SE Nicholson, U Novak, SF Ziegler and JE Layton
Melbourne Tumour Biology Branch, Ludwig Institute for Cancer Research,
Victoria Australia.
The protein tyrosine kinases JAK1 and JAK2 are phosphorylated tyrosine
after the interaction of granulocyte colony-stimulating factor (G-CSF) with
its transmembrane receptor. So too is Stat3, a member of the STAT family of
transcriptional activators thought to be activated by the JAK kinases.
Truncated G-CSF receptor (G-CSF-R) mutants were used to determine the
different regions of the cytoplasmic domain necessary for tyrosine
phosphorylation of the signaling molecules JAK2, Stat3, and p42, p44MAPK.
We have shown that G-CSF-induced tyrosine phosphorylation and kinase
activation of JAK2 requires the membrane proximal 57 amino acids of the
cytoplasmic domain. In contrast, maximal Stat3 tyrosine phosphorylation
required amino acids 96 to 183 of the G-CSF-R cytoplasmic domain, Stat3 DNA
binding could occur with a receptor truncated 96 amino acids from the
transmembrane domain and containing a single tyrosine residue, but was
reduced in comparison with the full- length receptor. Together with the
tyrosine phosphorylation of Stat3, this finding suggests that additional
Stat3 does not appear to be required for proliferation. MAP kinase tyrosine
phosphorylation correlated with both the proliferative response and JAK2
activation.
Volume 86,
Issue 10,
pp. 3698-3704,
11/15/1995
Copyright © 1995 by The American Society of Hematology
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