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Genes & Dev. 14 (18): 2314-2329

Copyright © 2000 by Cold Spring Harbor Laboratory Press.

Vol. 14, No. 18, pp. 2314-2329, September 15, 2000

RESEARCH PAPER
The glucocorticoid receptor inhibits NFkappa B by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain

Robert M. Nissen, and Keith R. Yamamoto1

Departments of Cellular and Molecular Pharmacology, and Biochemistry and Biophysics, PIBS Biochemistry and Molecular Biology Program, University of California, San Francisco, San Francisco, California 94143-0450, USA

Glucocorticoids repress NFkappa B-mediated activation of proinflammatory genes such as interleukin-8 (IL-8) and ICAM-1. Our experiments suggest that the glucocorticoid receptor (GR) confers this effect by associating through protein-protein interactions with NFkappa B bound at each of these genes. That is, we show that the GR zinc binding region (ZBR), which includes the DNA binding and dimerization functions of the receptor, binds directly to the dimerization domain of the RelA subunit of NFkappa B in vitro and that the ZBR is sufficient to associate with RelA bound at NFkappa B response elements in vivo. Moreover, we demonstrate in vivo and in vitro that GR does not disrupt DNA binding by NFkappa B. In transient transfections, we found that the GR ligand binding domain is essential for repression of NFkappa B but not for association with it and that GR can repress an NFkappa B derivative bearing a heterologous activation domain. We used chromatin immunoprecipitation assays in untransfected A549 cells to infer the mechanism by which the tethered GR represses NFkappa B-activated transcription. As expected, we found that the inflammatory signal TNFalpha stimulated preinitiation complex (PIC) assembly at the IL-8 and ICAM-1 promoters and that the largest subunit of RNA polymerase II (pol II) in those complexes became phosphorylated at serines 2 and 5 in its carboxy-terminal domain (CTD) heptapeptide repeats (YSPTSPS); these modifications are required for transcription initiation. Remarkably, GR did not inhibit PIC assembly under repressing conditions, but rather interfered with phosphorylation of serine 2 of the pol II CTD.

[Key Words: Glucocorticoid receptor; transcriptional repression; intracellular receptor; RelA; chromatin; anti-inflammation]

1 Corresponding author.

GENES & DEVELOPMENT 14:2314-2329 © 2000 by Cold Spring Harbor Laboratory Press  ISSN 0890-9369/00 $5.00

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Y. Tian, S. Ke, M. Chen, and T. Sheng (2003)
J. Biol. Chem. 278, 44041-44048
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Dexamethasone Enhances Osteoclast Formation Synergistically with Transforming Growth Factor-{beta} by Stimulating the Priming of Osteoclast Progenitors for Differentiation into Osteoclasts.
A. Takuma, T. Kaneda, T. Sato, S. Ninomiya, M. Kumegawa, and Y. Hakeda (2003)
J. Biol. Chem. 278, 44667-44674
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Agonist and Chemopreventative Ligands Induce Differential Transcriptional Cofactor Recruitment by Aryl Hydrocarbon Receptor.
E. V. Hestermann and M. Brown (2003)
Mol. Cell. Biol. 23, 7920-7925
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Identification of Glucocorticoid Receptor Domains Involved in Transrepression of Transforming Growth Factor-{beta} Action.
G. Li, S. Wang, and T. D. Gelehrter (2003)
J. Biol. Chem. 278, 41779-41788
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Functional Analysis of Three Genetic Polymorphisms in the Glucocorticoid Receptor Gene.
S. Koyano, Y. Saito, M. Nagano, K. Maekawa, Y. Kikuchi, N. Murayama, T. Fujino, S. Ozawa, T. Nakajima, K. Matsumoto, et al. (2003)
J. Pharmacol. Exp. Ther. 307, 110-116
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The Interplay between the Glucocorticoid Receptor and Nuclear Factor-{kappa}B or Activator Protein-1: Molecular Mechanisms for Gene Repression.
K. De Bosscher, W. Vanden Berghe, and G. Haegeman (2003)
Endocr. Rev. 24, 488-522
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