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Department of Physiology (N.K., J.J.P., O.A.J.) Institute of
Biomedicine University of Helsinki FIN-00014 Helsinki,
Finland
Department of Clinical Chemistry (O.A.J.)
University of Helsinki FIN-00290 Helsinki, Finland
Department of Medical Biochemistry (S.A., O.S.) University of
Tampere and Tampere University Hospital FIN-33014 Tampere,
Finland
Steroid receptors mediate their actions by using
various coregulatory proteins. We have recently characterized
ARIP3/PIASx
as an androgen receptor (AR)-interacting protein (ARIP)
that belongs to the PIAS [protein inhibitor of activated STAT
(signal transducer and activator of transcription)] protein family
implicated in the inhibition of cytokine signaling. We have analyzed
herein the roles that four different PIAS proteins (ARIP3/PIASx
,
Miz1/PIASxß, GBP/PIAS1, and PIAS3) play in the regulation of steroid
receptor- or STAT-mediated transcriptional activation. All PIAS
proteins are able to coactivate steroid receptor-dependent
transcription but to a differential degree, depending on the receptor,
the promoter, and the cell type. Miz1 and PIAS1 are more potent than
ARIP3 in activating AR function on minimal promoters. With the natural
probasin promoter, PIAS proteins influence AR function more
divergently, in that ARIP3 represses, but Miz1 and PIAS1 activate it.
Miz1 and PIAS1 possess inherent transcription activating function,
whereas ARIP3 and PIAS3 are devoid of this feature. ARIP3 enhances
glucocorticoid receptor-dependent transcription more efficiently than
Miz1 or PIAS1, and all PIAS proteins also activate estrogen receptor-
and progesterone receptor-dependent transcription but to a
dissimilar degree. The same amounts of PIAS proteins that modulate
steroid receptor-dependent transcription influence only marginally
transactivation mediated by various STAT proteins. It remains to be
established whether the PIAS proteins play a more significant
physiological role in steroid receptor than in cytokine signaling.
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M. Tojo, K. Matsuzaki, T. Minami, Y. Honda, H. Yasuda, T. Chiba, H. Saya, Y. Fujii-Kuriyama, and M. Nakao The Aryl Hydrocarbon Receptor Nuclear Transporter Is Modulated by the SUMO-1 Conjugation System J. Biol. Chem., November 22, 2002; 277(48): 46576 - 46585. [Abstract] [Full Text] [PDF] |
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M. I. Tussie-Luna, B. Michel, S. Hakre, and A. L. Roy The SUMO Ubiquitin-Protein Isopeptide Ligase Family Member Miz1/PIASxbeta /Siz2 Is a Transcriptional Cofactor for TFII-I J. Biol. Chem., November 1, 2002; 277(45): 43185 - 43193. [Abstract] [Full Text] [PDF] |
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T. Nishida and H. Yasuda PIAS1 and PIASxalpha Function as SUMO-E3 Ligases toward Androgen Receptor and Repress Androgen Receptor-dependent Transcription J. Biol. Chem., October 25, 2002; 277(44): 41311 - 41317. [Abstract] [Full Text] [PDF] |
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P. Li, X. Yu, K. Ge, J. Melamed, R. G. Roeder, and Z. Wang Heterogeneous Expression and Functions of Androgen Receptor Co-Factors in Primary Prostate Cancer Am. J. Pathol., October 1, 2002; 161(4): 1467 - 1474. [Abstract] [Full Text] [PDF] |
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Y. Le Drean, N. Mincheneau, P. Le Goff, and D. Michel Potentiation of Glucocorticoid Receptor Transcriptional Activity by Sumoylation Endocrinology, September 1, 2002; 143(9): 3482 - 3489. [Abstract] [Full Text] [PDF] |
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N. Kotaja, U. Karvonen, O. A. Janne, and J. J. Palvimo The Nuclear Receptor Interaction Domain of GRIP1 Is Modulated by Covalent Attachment of SUMO-1 J. Biol. Chem., August 9, 2002; 277(33): 30283 - 30288. [Abstract] [Full Text] [PDF] |
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T. Raivio, J. J. Palvimo, S. Kannisto, R. Voutilainen, and O. A. Janne Transactivation Assay for Determination of Glucocorticoid Bioactivity in Human Serum J. Clin. Endocrinol. Metab., August 1, 2002; 87(8): 3740 - 3744. [Abstract] [Full Text] [PDF] |
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N. Kotaja, U. Karvonen, O. A. Janne, and J. J. Palvimo PIAS Proteins Modulate Transcription Factors by Functioning as SUMO-1 Ligases Mol. Cell. Biol., July 15, 2002; 22(14): 5222 - 5234. [Abstract] [Full Text] [PDF] |
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N. Kotaja, M. Vihinen, J. J. Palvimo, and O. A. Janne Androgen Receptor-interacting Protein 3 and Other PIAS Proteins Cooperate with Glucocorticoid Receptor-interacting Protein 1 in Steroid Receptor-dependent Signaling J. Biol. Chem., May 10, 2002; 277(20): 17781 - 17788. [Abstract] [Full Text] [PDF] |
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B. A. Wible, L. Wang, Y. A. Kuryshev, A. Basu, S. Haldar, and A. M. Brown Increased K+ Efflux and Apoptosis Induced by the Potassium Channel Modulatory Protein KChAP/PIAS3beta in Prostate Cancer Cells J. Biol. Chem., May 10, 2002; 277(20): 17852 - 17862. [Abstract] [Full Text] [PDF] |
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J.-A. Tan, S. H. Hall, K. G. Hamil, G. Grossman, P. Petrusz, and F. S. French Protein Inhibitors of Activated STAT Resemble Scaffold Attachment Factors and Function as Interacting Nuclear Receptor Coregulators J. Biol. Chem., May 3, 2002; 277(19): 16993 - 17001. [Abstract] [Full Text] [PDF] |
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C.-Y. Chang and D. P. McDonnell Evaluation of Ligand-Dependent Changes in AR Structure Using Peptide Probes Mol. Endocrinol., April 1, 2002; 16(4): 647 - 660. [Abstract] [Full Text] [PDF] |
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E. Holter, N. Kotaja, S. Makela, L. Strauss, S. Kietz, O. A. Janne, J.-A. Gustafsson, J. J. Palvimo, and E. Treuter Inhibition of Androgen Receptor (AR) Function by the Reproductive Orphan Nuclear Receptor DAX-1 Mol. Endocrinol., March 1, 2002; 16(3): 515 - 528. [Abstract] [Full Text] [PDF] |
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D. Schmidt and S. Muller Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity PNAS, February 20, 2002; (2002) 52559499. [Abstract] [Full Text] [PDF] |
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M. Kobayashi, S. Kishida, A. Fukui, T. Michiue, Y. Miyamoto, T. Okamoto, Y. Yoneda, M. Asashima, and A. Kikuchi Nuclear Localization of Duplin, a beta -Catenin-binding Protein, Is Essential for Its Inhibitory Activity on the Wnt Signaling Pathway J. Biol. Chem., February 15, 2002; 277(8): 5816 - 5822. [Abstract] [Full Text] [PDF] |
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P. K. Jackson A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases Genes & Dev., December 1, 2001; 15(23): 3053 - 3058. [Full Text] [PDF] |
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S. Sachdev, L. Bruhn, H. Sieber, A. Pichler, F. Melchior, and R. Grosschedl PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies Genes & Dev., December 1, 2001; 15(23): 3088 - 3103. [Abstract] [Full Text] [PDF] |
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K. Takahashi, T. Taira, T. Niki, C. Seino, S. M. M. Iguchi-Ariga, and H. Ariga DJ-1 Positively Regulates the Androgen Receptor by Impairing the Binding of PIASxalpha to the Receptor J. Biol. Chem., September 28, 2001; 276(40): 37556 - 37563. [Abstract] [Full Text] [PDF] |
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M. D. Zentner, H. H. Lin, H.-T. Deng, K.-J. Kim, H.-M. Shih, and D. K. Ann Requirement for High Mobility Group Protein HMGI-C Interaction with STAT3 Inhibitor PIAS3 in Repression of alpha -Subunit of Epithelial Na+ Channel (alpha -ENaC) Transcription by Ras Activation in Salivary Epithelial Cells J. Biol. Chem., August 3, 2001; 276(32): 29805 - 29814. [Abstract] [Full Text] [PDF] |