Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140

J Biol Chem. 2004 Apr 9;279(15):15645-51. doi: 10.1074/jbc.M313906200. Epub 2004 Jan 21.


Receptor interacting protein (RIP) 140 is a corepressor that can be recruited to nuclear receptors by means of LXXLL motifs. We have characterized four distinct autonomous repression domains in RIP140, termed RD1-4, that are highly conserved in mammals and birds. RD1 at the N terminus represses transcription in the presence of trichostatin A, suggesting that it functions by a histone deacetylase (HDAC)-independent mechanism. The repressive activity of RD2 is dependent upon carboxyl-terminal binding protein recruitment to two specific binding sites. Use of specific inhibitors indicates that RD2, RD3, and RD4 are capable of functioning by HDAC-dependent and HDAC-independent mechanisms, depending upon cell type.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CHO Cells
  • COS Cells
  • Cell Line
  • Cricetinae
  • Glutathione Transferase / metabolism
  • Histone Deacetylases / metabolism
  • Humans
  • Hydroxamic Acids / pharmacology
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry*
  • Nuclear Receptor Interacting Protein 1
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Transfection


  • Adaptor Proteins, Signal Transducing
  • Hydroxamic Acids
  • NRIP1 protein, human
  • Nuclear Proteins
  • Nuclear Receptor Interacting Protein 1
  • Recombinant Fusion Proteins
  • trichostatin A
  • Glutathione Transferase
  • Histone Deacetylases