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Science 25 June 1999:
Vol. 284. no. 5423, pp. 2174 - 2177
DOI: 10.1126/science.284.5423.2174
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Reports

Regulation of Transcription by a Protein Methyltransferase

Dagang Chen, 1 Han Ma, 1 Heng Hong, 1 Stephen S. Koh, 1 Shih-Ming Huang, 1 Brandon T. Schurter, 2 Dana W. Aswad, 2 Michael R. Stallcup 1*

The p160 family of coactivators, SRC-1, GRIP1/TIF2, and p/CIP, mediate transcriptional activation by nuclear hormone receptors. Coactivator-associated arginine methyltransferase 1 (CARM1), a previously unidentified protein that binds to the carboxyl-terminal region of p160 coactivators, enhanced transcriptional activation by nuclear receptors, but only when GRIP1 or SRC-1a was coexpressed. Thus, CARM1 functions as a secondary coactivator through its association with p160 coactivators. CARM1 can methylate histone H3 in vitro, and a mutation in the putative S-adenosylmethionine binding domain of CARM1 substantially reduced both methyltransferase and coactivator activities. Thus, coactivator-mediated methylation of proteins in the transcription machinery may contribute to transcriptional regulation.

1 Department of Pathology HMR 301, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033, USA.
2 Department of Biochemistry and Molecular Biology, University of California, Biosciences II, Room 3205, Irvine, CA 92697, USA.
*   To whom correspondence should be addressed. E-mail: stallcup{at}hsc.usc.edu

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Signal-dependent Control of Gluconeogenic Key Enzyme Genes through Coactivator-associated Arginine Methyltransferase 1.
A. Krones-Herzig, A. Mesaros, D. Metzger, A. Ziegler, U. Lemke, J. C. Bruning, and S. Herzig (2006)
J. Biol. Chem. 281, 3025-3029
   Abstract »    Full Text »    PDF »
Differential Use of Functional Domains by Coiled-coil Coactivator in Its Synergistic Coactivator Function with beta-Catenin or GRIP1.
C. K. Yang, J. H. Kim, H. Li, and M. R. Stallcup (2006)
J. Biol. Chem. 281, 3389-3397
   Abstract »    Full Text »    PDF »
Downstream signaling mechanism of the C-terminal activation domain of transcriptional coactivator CoCoA..
J. H. Kim, C. K. Yang, and M. R. Stallcup (2006)
Nucleic Acids Res. 34, 2736-2750
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Scaffold attachment factor B1 directly interacts with nuclear receptors in living cells and represses transcriptional activity.
M-B Debril, L Dubuquoy, J-N Feige, W Wahli, B Desvergne, J Auwerx, and L Gelman (2005)
J. Mol. Endocrinol. 35, 503-517
   Abstract »    Full Text »    PDF »
Histone-Modifying Complexes Regulate Gene Expression Pertinent to the Differentiation of the Protozoan Parasite Toxoplasma gondii.
N. Saksouk, M. M. Bhatti, S. Kieffer, A. T. Smith, K. Musset, J. Garin, W. J. Sullivan Jr., M.-F. Cesbron-Delauw, and M.-A. Hakimi (2005)
Mol. Cell. Biol. 25, 10301-10314
   Abstract »    Full Text »    PDF »
The Nuclear Xenobiotic Receptor Pregnane X Receptor: Recent Insights and New Challenges.
J. Orans, D. G. Teotico, and M. R. Redinbo (2005)
Mol. Endocrinol. 19, 2891-2900
   Abstract »    Full Text »    PDF »
Dynamics of Human Protein Arginine Methyltransferase 1(PRMT1) in Vivo.
F. Herrmann, J. Lee, M. T. Bedford, and F. O. Fackelmayer (2005)
J. Biol. Chem. 280, 38005-38010
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Interplay among coactivator-associated arginine methyltransferase 1, CBP, and CIITA in IFN-{gamma}-inducible MHC-II gene expression.
E. Zika, L. Fauquier, L. Vandel, and J. P.-Y. Ting (2005)
PNAS 102, 16321-16326
   Abstract »    Full Text »    PDF »
Peptidyl-Prolyl Isomerase 1 (Pin1) Serves as a Coactivator of Steroid Receptor by Regulating the Activity of Phosphorylated Steroid Receptor Coactivator 3 (SRC-3/AIB1).
P. Yi, R.-C. Wu, J. Sandquist, J. Wong, S. Y. Tsai, M.-J. Tsai, A. R. Means, and B. W. O'Malley (2005)
Mol. Cell. Biol. 25, 9687-9699
   Abstract »    Full Text »    PDF »
The Ca2+-induced methyltransferase xPRMT1b controls neural fate in amphibian embryo.
J. Batut, L. Vandel, C. Leclerc, C. Daguzan, M. Moreau, and I. Neant (2005)
PNAS 102, 15128-15133
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PRMT8, a New Membrane-bound Tissue-specific Member of the Protein Arginine Methyltransferase Family.
J. Lee, J. Sayegh, J. Daniel, S. Clarke, and M. T. Bedford (2005)
J. Biol. Chem. 280, 32890-32896
   Abstract »    Full Text »    PDF »
SRC-3 Is Required for Prostate Cancer Cell Proliferation and Survival.
H.-J. Zhou, J. Yan, W. Luo, G. Ayala, S.-H. Lin, H. Erdem, M. Ittmann, S. Y. Tsai, and M.-J. Tsai (2005)
Cancer Res. 65, 7976-7983
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