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J. Biol. Chem., Vol. 269, Issue 7, 4701-4704, 02, 1994
DJ Meyer, GS Campbell, BH Cochran, LS Argetsinger, AC Larner, DS Finbloom, C Carter-Su and J Schwartz
Signaling mechanisms leading to regulation of gene transcription by growth
hormone (GH) and other molecules that signal via the cytokine receptor
family have been elusive. Based upon recent findings that GH and
interferons activate JAK family tyrosine kinases, we have identified a
novel signaling pathway leading from the GH receptor to the nucleus. We
report that in 3T3-F442A fibroblasts, GH stimulates tyrosyl phosphorylation
of a protein recognized by antibody to p91, a component of DNA-binding
complexes that are activated by tyrosyl phosphorylation in response to
interferons alpha and gamma. In addition, a GH-inducible DNA binding factor
(GHIF) is identified that binds to the c-sis-inducible element of the c-fos
promoter. GHIF contains a protein antigenically related to p91 and is
tyrosyl- phosphorylated. These findings indicate that in signaling between
their receptors and the nucleus, GH and interferons utilize related or
identical components, including JAK family tyrosine kinases and proteins in
the p91 family. When combined with recent findings that many members of the
cytokine receptor family activate JAK kinases, including some cytokines
that activate p91-related proteins, these findings suggest that signaling
pathways involving JAK kinases and p91 family members may be broadly
distributed.
Growth hormone induces a DNA binding factor related to the interferon- stimulated 91-kDa transcription factor
Department of Physiology, University of Michigan Medical School, Ann Arbor 48109.
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L. H. Hansen, X. Wang, J. J. Kopchick, P. Bouchelouche, J. H. Nielsen, E. D. Galsgaard, and N. Billestrup Identification of Tyrosine Residues in the Intracellular Domain of the Growth Hormone Receptor Required for Transcriptional Signaling and Stat5 Activation J. Biol. Chem., May 24, 1996; 271(21): 12669 - 12673. [Abstract] [Full Text] [PDF]
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P. E. Lobie, G. Allevato, J. H. Nielsen, G. Norstedt, and N. Billestrup Requirement of Tyrosine Residues 333 and 338 of the Growth Hormone (GH) Receptor for Selected GH-stimulated Function J. Biol. Chem., September 15, 1995; 270(37): 21745 - 21750. [Abstract] [Full Text] [PDF]
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R. H. Hackett, Y.-D. Wang, and A. C. Larner Mapping of the Cytoplasmic Domain of the Human Growth Hormone Receptor Required for the Activation of Jak2 and Stat Proteins J. Biol. Chem., September 8, 1995; 270(36): 21326 - 21330. [Abstract] [Full Text] [PDF]
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 C. Yu, D. Meyer, G. Campbell, A. Larner, C Carter-Su, J Schwartz, and R Jove Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein Science, July 7, 1995; 269(5220): 81 - 83. [Abstract] [PDF]
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L. S. Argetsinger, G. W. Hsu, M. G. Myers Jr., N. Billestrup, M. F. White, and C. Carter-Su Growth Hormone, Interferon-[IMAGE], and Leukemia Inhibitory Factor Promoted Tyrosyl Phosphorylation of Insulin Receptor Substrate-1 J. Biol. Chem., June 16, 1995; 270(24): 14685 - 14692. [Abstract] [Full Text] [PDF]
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