Journal article

DISTINCT REGIONS OF THE GRANULOCYTE-COLONY-STIMULATING FACTOR-RECEPTOR ARE REQUIRED FOR TYROSINE PHOSPHORYLATION OF THE SIGNALING MOLECULES JAK2, STAT3, AND P42, P44(MAPK)

SE NICHOLSON, U NOVAK, SF ZIEGLER, LE LAYTON

Blood | W B SAUNDERS CO | Published : 1995

Abstract

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 tyrosin..

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University of Melbourne Researchers