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J Biol Chem, Vol. 274, Issue 25, 18121-18127, June 18, 1999
From the Department of Recent development in the field of gene
regulation by nuclear receptors (NRs) have identified a role for
cofactors in transcriptional control. While some of the NR-associated
proteins serve as coactivators, the effect of the receptor interacting
protein 140 (RIP140) on NR transcriptional responses is complex. In
this report we have studied the effect of RIP140 on gene regulation by
the glucocorticoid receptor (GR). We demonstrate that RIP140
antagonized all GR-mediated responses tested, which included activation
through classical GRE, the synergistic effects of glucocorticoids on
AP-1 and Pbx1/HOXB1 responsive elements, as well as gene repression
through a negative GRE and cross-talk with NF-
Receptor Interacting Protein RIP140 Inhibits Both Positive and
Negative Gene Regulation by Glucocorticoids
,
Medical Nutrition,
§ Center for Biotechnology, Karolinska Institutet, Huddinge
University Hospital, F60 Novum, SE-141 86 Huddinge, Sweden
B (RelA). This
involved the ligand-binding domain of the GR and did not occur when the
GR was bound to the antagonist RU486. The strong repressive effect of
RIP140 was restricted to glucocorticoid-mediated responses in as much
as it slightly increased signaling through the RelA and the Pit-1/Pbx
proteins and only slightly repressed signaling through the Pbx1/HOXB1
and AP-1 proteins, excluding general squelching as a mechanism.
Instead, this suggests that RIP140 acts as a direct inhibitor of GR
function. In line with a direct effect of RIP140 on the GR, we
demonstrate a GR-RIP140 interaction in vitro by a
glutathione S-transferase-pull down assay. Furthermore, the
repressive effect of RIP140 could partially be overcome by
overexpression of the coactivator TIF2, which involved a competition
between TIF2 and RIP140 for binding to the GR.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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