[HTML][HTML] Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140
M Christian, JMA Tullet, MG Parker - Journal of Biological Chemistry, 2004 - ASBMB
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 …
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 …