Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Academic Article uri icon

Overview

abstract

  • The transcriptional corepressors SMRT and N-CoR function as silencing mediators for retinoid and thyroid hormone receptors. Here we show that SMRT and N-CoR directly interact with mSin3A, a corepressor for the Mad-Max heterodimer and a homolog of the yeast global-transcriptional repressor Sin3p. In addition, we demonstrate that the recently characterized histone deacetylase 1 (HDAC1) interacts with Sin3A and SMRT to form a multisubunit repressor complex. Consistent with this model, we find that HDAC inhibitors synergize with retinoic acid to stimulate hormone-responsive genes and differentiation of myeloid leukemia (HL-60) cells. This work establishes a convergence of repression pathways for bHLH-Zip proteins and nuclear receptors and suggests this type of regulation may be more widely conserved than previously suspected.

publication date

  • May 2, 1997

Research

keywords

  • DNA-Binding Proteins
  • Histone Deacetylases
  • Receptors, Cytoplasmic and Nuclear
  • Repressor Proteins
  • Transcription Factors

Identity

Scopus Document Identifier

  • 0030953186

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)80218-4

PubMed ID

  • 9150137

Additional Document Info

volume

  • 89

issue

  • 3