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Colony-stimulating factor 1-induced STAT1 and STAT3 activation is
accompanied by phosphorylation of Tyk2 in macrophages and Tyk2 and JAK1 in
fibroblasts
U Novak, AG Harpur, L Paradiso, V Kanagasundaram, A Jaworowski, AF Wilks and JA Hamilton
University of Melbourne, Department of Medicine, Royal Melbourne Hospital,
Parkville, Australia.
Colony-stimulating factor 1 (CSF-1) causes the activation of STAT1 and
STAT3 transcription factors in bone marrow macrophages (BMM), in the
macrophage cell line BAC1.2F5, and in fibroblasts that express the wild-
type receptor for CSF-1. Fibroblasts expressing a mutant receptor in which
the tyrosine 809 is replaced with phenylalanine do not activate STAT
proteins in response to CSF-1. The activation of the STAT proteins in BMM
is accompanied by tyrosine phosphorylation of Tyk2. In fibroblasts, the
activation of the STAT proteins is accompanied by tyrosine phosphorylation
of Tyk2 and JAK1. We propose that these JAK kinases are subjected to very
rapid phosphorylation in response to CSF- 1, followed by rapid
dephosphorylation. Furthermore, we propose that kinases other than JAK
kinase may be involved in the phosphorylation of the STAT proteins in
response to CSF-1.
Volume 86,
Issue 8,
pp. 2948-2956,
10/15/1995
Copyright © 1995 by The American Society of Hematology
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