Receptor interacting protein 140 as a thyroid hormone-dependent, negative co-regulator for the induction of cellular retinoic acid binding protein I gene

Li-Na Wei, Xinli Hu

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Over-expression of receptor interacting protein 140 (RIP140) suppressed thyroid hormone (T3) induction of cellular retinoic acid binding I protein (CRABPI) gene in P19 embryonal carcinoma cells. CRABPI induction by T3 is mediated by a direct-repeat four-element bound by T3 receptor (T3R) and retinoid receptor X (RXR). Three receptor-interacting domains (RIDs) in RIP140 mediate its interaction with T3R: one constitutive RID within the amino terminus, and two T3-dependent RIDs in the central portion and the carboxyl terminus. In co-immunoprecipitation and chromatin immunoprecipitation assays, RIP140 formed complexes with T3R/RXR in solution and on the endogenous target, the CRABPI promoter. T3 treatment resulted in elevated histone acetylation of the endogenous CRABPI gene promoter, but simultaneous expression of RIP140 resulted in significantly reduced histone acetylation of this promoter, primarily through the recruitment of HDAC4. This study presents the first evidence that over-expressed RIP140 acts as a T3-dependent negative co-regulator for T3 induction of the endogenous CRABPI gene in P19 cells.

Original languageEnglish (US)
Pages (from-to)39-48
Number of pages10
JournalMolecular and Cellular Endocrinology
Volume218
Issue number1-2
DOIs
StatePublished - Apr 15 2004

Bibliographical note

Funding Information:
This work was supported, in part, by grants DK54733, DK60521, K02-DA13926, DA11190 and DA11806 from the NIH to LNW.

Keywords

  • CRABPI
  • Histone acetylation
  • RIP140
  • Thyroid hormone
  • Thyroid hormone receptor

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