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Science 5 December 1997:
Vol. 278. no. 5344, pp. 1803 - 1805
DOI: 10.1126/science.278.5344.1803
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Reports

Specific Inhibition of Stat3 Signal Transduction by PIAS3

Chan D. Chung, * Jiayu Liao, * Bin Liu, Xiaoping Rao, Philippe Jay, Philippe Berta, Ke Shuai dagger

The signal transducer and activator of transcription-3 (Stat3) protein is activated by the interleukin 6 (IL-6) family of cytokines, epidermal growth factor, and leptin. A protein named PIAS3 (protein inhibitor of activated STAT) that binds to Stat3 was isolated and characterized. The association of PIAS3 with Stat3 in vivo was only observed in cells stimulated with ligands that cause the activation of Stat3. PIAS3 blocked the DNA-binding activity of Stat3 and inhibited Stat3-mediated gene activation. Although Stat1 is also phosphorylated in response to IL-6, PIAS3 did not interact with Stat1 or affect its DNA-binding or transcriptional activity. The results indicate that PIAS3 is a specific inhibitor of Stat3.

C. D. Chung and J. Liao, Department of Biological Chemistry, University of California, Los Angeles, CA 90095, USA.
B. Liu and X. Rao, Division of Hematology-Oncology, Department of Medicine, University of California, Los Angeles, CA 90095, USA.
P. Jay and P. Berta, Centre de Recherche de Biochimie Macromoleculaire, 1919 route de Mende, 34000 Montpellier, France.
K. Shuai, Division of Hematology-Oncology, Department of Medicine; Department of Biological Chemistry; and Molecular Biology Institute, University of California, 11-934 Factor Building, 10833 LeConte Avenue, Los Angeles, CA 90095-1678, USA.
*   These authors contributed equally to this manuscript.

dagger    To whom correspondence should be addressed.

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Y. Takahashi, A. Toh-e, and Y. Kikuchi (2003)
J. Biochem. 133, 415-422
   Abstract »    Full Text »    PDF »
The Role of Interleukin-6 in Nociception and Pain.
R. F. De Jongh, K. C. Vissers, T. F. Meert, L. H. D. J. Booij, C. S. De Deyne, and R. J. Heylen (2003)
Anesth. Analg. 96, 1096-1103
   Abstract »    Full Text »    PDF »
Tip60 Is a Co-repressor for STAT3.
H. Xiao, J. Chung, H.-Y. Kao, and Y.-C. Yang (2003)
J. Biol. Chem. 278, 11197-11204
   Abstract »    Full Text »    PDF »
The Drosophila trithorax group gene tonalli(tna) interacts genetically with the Brahma remodeling complex and encodes an SP-RING finger protein.
L. Gutierrez, M. Zurita, J. A. Kennison, and M. Vazquez (2003)
Development 130, 343-354
   Abstract »    Full Text »    PDF »
Interleukins in Atherosclerosis: Molecular Pathways and Therapeutic Potential.
J. H. Von der Thusen, J. Kuiper, T. J. C. Van Berkel, and E. A. L. Biessen (2003)
Pharmacol. Rev. 55, 133-166
   Abstract »    Full Text »    PDF »
The Growth Hormone-binding Protein Is a Location-dependent Cytokine Receptor Transcriptional Enhancer.
R. Graichen, J. Sandstedt, E. L. K. Goh, O. G. P. Isaksson, J. Tornell, and P. E. Lobie (2003)
J. Biol. Chem. 278, 6346-6354
   Abstract »    Full Text »    PDF »
The Role of Prolactin in Mammary Carcinoma.
C. V. Clevenger, P. A. Furth, S. E. Hankinson, and L. A. Schuler (2003)
Endocr. Rev. 24, 1-27
   Abstract »    Full Text »    PDF »
DJBP: A Novel DJ-1-Binding Protein, Negatively Regulates the Androgen Receptor by Recruiting Histone Deacetylase Complex, and DJ-1 Antagonizes This Inhibition by Abrogation of This Complex.
T. Niki, K. Takahashi-Niki, T. Taira, S. M.M. Iguchi-Ariga, and H. Ariga (2003)
Mol. Cancer Res. 1, 247-261
   Abstract »    Full Text »    PDF »
Expression and DNA-Binding Activity of Signal Transducer and Activator of Transcription 3 in Alcoholic Cirrhosis Compared to Normal Liver and Primary Biliary Cirrhosis in Humans.
P. Starkel, K. Bishop, Y. Horsmans, and A. J. Strain (2003)
Am. J. Pathol. 162, 587-596
   Abstract »    Full Text »    PDF »
Sumoylation of Mdm2 by Protein Inhibitor of Activated STAT (PIAS) and RanBP2 Enzymes.
Y. Miyauchi, S. Yogosawa, R. Honda, T. Nishida, and H. Yasuda (2002)
J. Biol. Chem. 277, 50131-50136
   Abstract »    Full Text »    PDF »
SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei.
T. R. Wu, Y. K. Hong, X.-D. Wang, M. Y. Ling, A. M. Dragoi, A. S. Chung, A. G. Campbell, Z.-Y. Han, G.-S. Feng, and Y. E. Chin (2002)
J. Biol. Chem. 277, 47572-47580
   Abstract »    Full Text »    PDF »
The SUMO Ubiquitin-Protein Isopeptide Ligase Family Member Miz1/PIASxbeta /Siz2 Is a Transcriptional Cofactor for TFII-I.
M. I. Tussie-Luna, B. Michel, S. Hakre, and A. L. Roy (2002)
J. Biol. Chem. 277, 43185-43193
   Abstract »    Full Text »    PDF »
PIAS1 and PIASxalpha Function as SUMO-E3 Ligases toward Androgen Receptor and Repress Androgen Receptor-dependent Transcription.
T. Nishida and H. Yasuda (2002)
J. Biol. Chem. 277, 41311-41317
   Abstract »    Full Text »    PDF »
Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta.
M. I. Tussie-Luna, D. Bayarsaihan, E. Seto, F. H. Ruddle, and A. L. Roy (2002)
PNAS 99, 12807-12812
   Abstract »    Full Text »    PDF »
Analysis of the Life Cycle of Stat6. CONTINUOUS CYCLING OF STAT6 IS REQUIRED FOR IL-4 SIGNALING.
R. P. Andrews, M. B. Ericksen, C. M. Cunningham, M. O. Daines, and G. K. K. Hershey (2002)
J. Biol. Chem. 277, 36563-36569
   Abstract »    Full Text »    PDF »


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