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Science 7 August 1992:
Vol. 257. no. 5071, pp. 809 - 813
DOI: 10.1126/science.1496401
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Articles

Science, Vol 257, Issue 5071, 809-813
Copyright © 1992 by American Association for the Advancement of Science

articles

Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor

C Schindler, K Shuai, VR Prezioso, and JE Darnell Jr

Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.

The interferon-alpha (IFN-alpha)-stimulated gene factor 3 (ISGF3), a transcriptional activator, contains three proteins, termed ISGF3 alpha proteins, that reside in the cell cytoplasm until they are activated in response to IFN-alpha. Treatment of cells with IFN-alpha caused these three proteins to be phosphorylated on tyrosine and to translocate to the cell nucleus where they stimulate transcription through binding to IFN-alpha-stimulated response elements in DNA. IFN-gamma, which activates transcription through a different receptor and different DNA binding sites, also caused tyrosine phosphorylation of one of these proteins. The ISGF3 alpha proteins may be substrates for one or more kinases activated by ligand binding to the cell surface and may link occupation of a specific polypeptide receptor with activation of transcription of a set of specific genes.


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D. Wang, J. Zamorano, A. D. Keegan, and M. Boothby (1997)
J. Biol. Chem. 272, 25083-25090
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Signal Transducer and Activator of Transcription-3 Serine Phosphorylation by Insulin Is Mediated by a Ras/Raf/MEK-Dependent Pathway.
B. P. Ceresa, C. M. Horvath, and J. E. Pessin (1997)
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Janus Kinase-dependent Activation of Insulin Receptor Substrate 1 in Response to Interleukin-4, Oncostatin M, and the Interferons.
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Regulation of Interferon-alpha Responsiveness by the Duration of Janus Kinase Activity.
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Molecular Cloning of a New Interferon-induced PML Nuclear Body-associated Protein.
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J. Biol. Chem. 272, 4600-4605
   Abstract »    Full Text »    PDF »
Interferon gamma -dependent Induction of Human Intercellular Adhesion Molecule-1 Gene Expression Involves Activation of a Distinct STAT Protein Complex.
S. M. Naik, N. Shibagaki, L.-J. Li, K. L. Quinlan, L. L.L. Paxton, and S. W. Caughman (1997)
J. Biol. Chem. 272, 1283-1290
   Abstract »    Full Text »    PDF »
Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution.
T Cao, K. Borden, P. Freemont, and L. Etkin (1997)
J. Cell Sci. 110, 1563-1571
   Abstract »    PDF »
Two contact regions between Stat1 and CBP/p300 in interferon gamma  signaling.
J. J. Zhang, U. Vinkemeier, W. Gu, D. Chakravarti, C. M. Horvath, and J. E. Darnell Jr. (1996)
PNAS 93, 15092-15096
   Abstract »    Full Text »    PDF »
Nuclear Transport of Granzyme B (Fragmentin-2). DEPENDENCE ON PERFORIN IN VIVO AND CYTOSOLIC FACTORS IN VITRO.
D. A. Jans, P. Jans, L. J. Briggs, V. Sutton, and J. A. Trapani (1996)
J. Biol. Chem. 271, 30781-30789
   Abstract »    Full Text »    PDF »
A Negative Regulatory Region in the Intracellular Domain of the Human Interferon-alpha Receptor.
V. C. Gibbs, M. Takahashi, M. Aguet, and A. Chuntharapai (1996)
J. Biol. Chem. 271, 28710-28716
   Abstract »    Full Text »    PDF »
Differences in Interferon alpha and beta Signaling. INTERFERON beta SELECTIVELY INDUCES THE INTERACTION OF THE alpha AND beta L SUBUNITS OF THE TYPE I INTERFERON RECEPTOR.
L. C. Platanias, S. Uddin, P. Domanski, and O. R. Colamonici (1996)
J. Biol. Chem. 271, 23630-23633
   Abstract »    Full Text »    PDF »
Characterization of beta -R1, a Gene That Is Selectively Induced by Interferon beta (IFN-beta ) Compared with IFN-alpha.
M.R. S. Rani, G. R. Foster, S. Leung, D. Leaman, G. R. Stark, and R. M. Ransohoff (1996)
J. Biol. Chem. 271, 22878-22884
   Abstract »    Full Text »    PDF »
Interferon-gamma Induction of the Human Leukocyte Antigen-E Gene Is Mediated through Binding of a Complex Containing STAT1alpha to a Distinct Interferon-gamma -responsive Element.
K. S. Gustafson and G. D. Ginder (1996)
J. Biol. Chem. 271, 20035-20046
   Abstract »    Full Text »    PDF »
Formation of STAT5-containing DNA Binding Complexes in Response to Colony-stimulating Factor-1 and Platelet-derived Growth Factor.
U. Novak, A. Mui, A. Miyajima, and L. Paradiso (1996)
J. Biol. Chem. 271, 18350-18354
   Abstract »    Full Text »    PDF »
The SH2 Domain-containing Tyrosine Phosphatase PTP1D Is Required for Interferon alpha /beta -induced Gene Expression.
M. David, G. Zhou, R. Pine, J. E. Dixon, and A. C. Larner (1996)
J. Biol. Chem. 271, 15862-15865
   Abstract »    Full Text »    PDF »
Differential Activation of Acute Phase Response Factor/Stat3 and Stat1 via the Cytoplasmic Domain of the Interleukin 6 Signal Transducer gp130. II. Src HOMOLOGY SH2 DOMAINS DEFINE THE SPECIFICITY OF STAT FACTOR ACTIVATION.
U. Hemmann, C. Gerhartz, B. Heesel, J. Sasse, G. Kurapkat, J. Grotzinger, A. Wollmer, Z. Zhong, J. E. Darnell Jr., L. Graeve, et al. (1996)
J. Biol. Chem. 271, 12999-13007
   Abstract »    Full Text »    PDF »
Insulin Stimulates the Serine Phosphorylation of the Signal Transducer and Activator of Transcription (STAT3) Isoform.
B. P. Ceresa and J. E. Pessin (1996)
J. Biol. Chem. 271, 12121-12124
   Abstract »    Full Text »    PDF »
Application of Genomic DNA Affinity Chromatography Identifies Multiple Interferon-alpha-regulated Stat2 Complexes.
J. J. Ghislain and E. N. Fish (1996)
J. Biol. Chem. 271, 12408-12413
   Abstract »    Full Text »    PDF »
STAT3beta , a Splice Variant of Transcription Factor STAT3, Is a Dominant Negative Regulator of Transcription.
E. Caldenhoven (1996)
J. Biol. Chem. 271, 13221-13227
   Abstract »    Full Text »    PDF »
Direct Association of STAT3 with the IFNAR-1 Chain of the Human Type I Interferon Receptor.
C.-H. Yang, W. Shi, L. Basu, A. Murti, S. N. Constantinescu, L. Blatt, E. Croze, J. E. Mullersman, and L. M. Pfeffer (1996)
J. Biol. Chem. 271, 8057-8061
   Abstract »    Full Text »    PDF »


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