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Sentences for "corepressors "
In concert with the observation that corepressors are associated with HDAC activities [ 84 85 ] , it appears that the transcriptional outcome of nuclear receptors is determined by the balance of histone acetylation and deacetylation activities, and that ligands serve as a switch to recruit HATs with the concomitant dismissal of HDACs.
In the absence of cognate hormone, several nuclear receptors actively repress transcription of target genes via interactions with the nuclear receptor corepressors SMRT and NCoR.
Upon binding of the hormone, these corepressors dissociate from the DNA-bound receptor, which subsequently recruits a nuclear receptor coactivator (NCoA) complex.
RAR/RXR binding to nuclear receptor corepressors such as NCoR and SMRT in the absence of ligand inhibits activation of RA responsive genes [ 3 4 ] .
NR corepressors include NR corepressor (N-CoR) and silencing mediator of retinoid and thyroid responsive transcription (SMRT) [ 4 ] .
Other known NR corepressors include RIP140 [ 10 ] , Hairless [ 11 ] , short heterodimer partner (SHP) [ 12 ] and DAX [ 13 ] , and receptor specific corepressors such as the estrogen receptor (ER) interacting proteins REA and HET-SAFB [ 14 15 ] .
RIP140, Hairless and DAX possess NR boxes that interact with AF-2 [ 11 13 19 ] and these corepressors act as negative regulators of the activity of the liganded NR.
A HDAC Repressor Enhances ERß Activity Since ERß bound N-CoR and SMRT in the presence of estrogens, we investigated the possible involvement of corepressors in the actions of agonist-bound ERß in vivo .
This is consistent with the notion that corepressors restrict the activity of agonist-bound ERß-LBD.
Conclusions NRs generally interact with the corepressors N-CoR and SMRT either in the absence of ligand, or in the presence of receptor antagonists, and agonists promote corepressor release [ 4 ] .
The fact that the mode of ERß interaction with N-CoR resembles that of NRs with coactivators [ 4 ] , or with corepressors that modulate the activity of liganded NR complexes, such as RIP140 [ 10 ] , raises the possibility that ERß may be able to recruit N-CoR and SMRT to estrogen-regulated promoters in response to agonists and that the balance of overall ERß activity in the presence of estrogens may be regulated by competition between p160s and corepressors for the same ERß AF-2 surface.
Other aspects of ERß interactions with corepressors warrant further study.
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