PMID- 24962880
OWN - NLM
STAT- MEDLINE
DCOM- 20141118
LR  - 20140625
IS  - 0306-0225 (Print)
IS  - 0306-0225 (Linking)
VI  - 70
DP  - 2014
TI  - Retinoic acid receptors: structural basis for coregulator interaction and 
      exchange.
PG  - 37-54
LID - 10.1007/978-94-017-9050-5_3 [doi]
AB  - In the form of heterodimers with retinoid X receptors (RXRs), retinoic acid 
      receptors (RARs) are master regulators of gene expression in humans and important 
      drug targets. They act as ligand-dependent transcription factors that regulate a 
      large variety of gene networks controlling cell growth, differentiation, survival 
      and death. The biological functions of RARs rely on a dynamic series of 
      coregulator exchanges controlled by ligand binding. Unliganded RARs exert a 
      repressor activity by interacting with transcriptional corepressors which 
      themselves serve as docking platforms for the recruitment of histone deacetylases 
      that impose a higher order structure on chromatin which is not permissive to gene 
      transcription. Upon ligand binding, the receptor undergoes conformational changes 
      inducing corepressor release and the recruitment of coactivators with histone 
      acetylase activities allowing chromatin decompaction and gene transcription. In 
      the following, we review the structural determinants of the interaction between 
      RAR and either type of coregulators both at the level of the individual receptor 
      and in the context of the RAR-RXR heterodimers. We also discuss the molecular 
      details of the fine tuning of these associations by the various pharmacological 
      classes of ligands.
FAU - le Maire, Albane
AU  - le Maire A
AD  - Inserm U1054, Centre de Biochimie Structurale, 29 rue de Navacelles, 34090, 
      Montpellier, France, lemaire@cbs.cnrs.fr.
FAU - Bourguet, William
AU  - Bourguet W
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - Subcell Biochem
JT  - Sub-cellular biochemistry
JID - 0316571
RN  - 0 (Chromatin)
RN  - 0 (Ligands)
RN  - 0 (Protein Isoforms)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Retinoid X Receptors)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
SB  - IM
MH  - Chromatin/*chemistry/metabolism
MH  - *Gene Expression Regulation
MH  - Histone Acetyltransferases/genetics/metabolism
MH  - Humans
MH  - Ligands
MH  - Models, Molecular
MH  - Protein Binding
MH  - Protein Isoforms/chemistry/genetics/metabolism
MH  - Protein Multimerization
MH  - Protein Structure, Tertiary
MH  - Receptors, Retinoic Acid/*chemistry/genetics/metabolism
MH  - Response Elements
MH  - Retinoid X Receptors/*chemistry/genetics/metabolism
MH  - Signal Transduction
EDAT- 2014/06/26 06:00
MHDA- 2014/11/19 06:00
CRDT- 2014/06/26 06:00
PHST- 2014/06/26 06:00 [entrez]
PHST- 2014/06/26 06:00 [pubmed]
PHST- 2014/11/19 06:00 [medline]
AID - 10.1007/978-94-017-9050-5_3 [doi]
PST - ppublish
SO  - Subcell Biochem. 2014;70:37-54. doi: 10.1007/978-94-017-9050-5_3.