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PMID: 10995388 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain.

Genes & development ·Vol. 14 ·No. 18 ·2000-09-15 ·Pages 2314-29

Nissen RM, Yamamoto KR

Abstract

Glucocorticoids repress NFkappaB-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 NFkappaB 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 NFkappaB in vitro and that the ZBR is sufficient to associate with RelA bound at NFkappaB response elements in vivo. Moreover, we demonstrate in vivo and in vitro that GR does not disrupt DNA binding by NFkappaB. In transient transfections, we found that the GR ligand binding domain is essential for repression of NFkappaB but not for association with it and that GR can repress an NFkappaB 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 NFkappaB-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.

MeSH Terms
Cell Line Humans I-kappa B Proteins/genetics,metabolism Intercellular Adhesion Molecule-1/genetics,metabolism Interleukin-8/antagonists & inhibitors,genetics,metabolism NF-kappa B/antagonists & inhibitors,metabolism Phosphorylation Precipitin Tests Promoter Regions, Genetic Protein Binding Protein Structure, Tertiary RNA Polymerase II/metabolism Receptors, Glucocorticoid/physiology Repressor Proteins/physiology Response Elements Serine/metabolism Tumor Necrosis Factor-alpha/metabolism Zinc/metabolism
Chemicals
I-kappa B Proteins Interleukin-8 NF-kappa B Receptors, Glucocorticoid Repressor Proteins Tumor Necrosis Factor-alpha Intercellular Adhesion Molecule-1 Serine RNA Polymerase II Zinc
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Nissen R M
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.
Yamamoto K R
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Article Info
Journal
Genes & development
Abbr.
Genes Dev
ISSN
0890-9369
DOI
10.1101/gad.827900
Published
2000-09-15
Pages
2314-29
Language
English
Region
United States
NLM ID
8711660
PMCID
PMC316928
Subset
IM
External Links
PubMed source DOI: 10.1101/gad.827900 PMC Full Text View journal details
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