PMID- 15650024
OWN - NLM
STAT- MEDLINE
DCOM- 20050831
LR  - 20181113
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 19
IP  - 4
DP  - 2005 Apr
TI  - Heterodimers of retinoic acid receptors and thyroid hormone receptors display 
      unique combinatorial regulatory properties.
PG  - 863-78
AB  - Nuclear receptors are ligand-regulated transcription factors that regulate key 
      aspects of metazoan development, differentiation, and homeostasis. Nuclear 
      receptors recognize target genes by binding to specific DNA recognition 
      sequences, denoted hormone response elements (HREs). Many nuclear receptors can 
      recognize HREs as either homodimers or heterodimers. Retinoid X receptors (RXRs), 
      in particular, serve as important heterodimer partners for many other nuclear 
      receptors, including thyroid hormone receptors (TRs), and RXR/TR heterodimers 
      have been proposed to be the primary mediators of target gene regulation by T3 
      hormone. Here, we report that the retinoic acid receptors (RARs), a distinct 
      class of nuclear receptors, are also efficient heterodimer partners for TRs. 
      These RAR/TR heterodimers form with similar affinities as RXR/TR heterodimers on 
      an assortment of consensus and natural HREs, and preferentially assemble with the 
      RAR partner 5' of the TR moiety. The corepressor and coactivator recruitment 
      properties of these RAR/TR heterodimers and their transcriptional activities in 
      vivo are distinct from those observed with the corresponding RXR heterodimers. 
      Our studies indicate that RXRs are not unique in their ability to partner with 
      TRs, and that RARs can also serve as robust heterodimer partners and 
      combinatorial regulators of T3-modulated gene expression.
FAU - Lee, Sangho
AU  - Lee S
AD  - Section of Microbiology, One Shields Avenue, University of California at Davis, 
      Davis, California 95616, USA.
FAU - Privalsky, Martin L
AU  - Privalsky ML
LA  - eng
GR  - R37 CA053394/CA/NCI NIH HHS/United States
GR  - R01 DK053528-07/DK/NIDDK NIH HHS/United States
GR  - R01 DK053528/DK/NIDDK NIH HHS/United States
GR  - R37 CA53394/CA/NCI NIH HHS/United States
GR  - R01 DK053528-10/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20050113
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (RARA protein, human)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Retinoic Acid Receptor alpha)
RN  - 0 (Retinoid X Receptor gamma)
RN  - 0 (Thyroid Hormone Receptors alpha)
RN  - 0 (Transcription Factors)
RN  - 06LU7C9H1V (Triiodothyronine)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
RN  - EC 2.3.1.48 (NCOA1 protein, human)
RN  - EC 2.3.1.48 (Nuclear Receptor Coactivator 1)
RN  - EC 2.3.1.48 (Nuclear Receptor Coactivator 3)
SB  - IM
MH  - Animals
MH  - DNA-Binding Proteins/*metabolism
MH  - Dimerization
MH  - Genes, Reporter
MH  - Histone Acetyltransferases
MH  - Humans
MH  - Nuclear Receptor Coactivator 1
MH  - Nuclear Receptor Coactivator 3
MH  - Receptors, Retinoic Acid/*metabolism
MH  - Response Elements
MH  - Retinoic Acid Receptor alpha
MH  - Retinoid X Receptor gamma/*metabolism
MH  - Thyroid Hormone Receptors alpha/*metabolism
MH  - Transcription Factors/metabolism
MH  - *Transcriptional Activation
MH  - Triiodothyronine/metabolism
PMC - PMC2675561
MID - NIHMS92269
EDAT- 2005/01/15 09:00
MHDA- 2005/09/01 09:00
PMCR- 2009/04/30
CRDT- 2005/01/15 09:00
PHST- 2005/01/15 09:00 [pubmed]
PHST- 2005/09/01 09:00 [medline]
PHST- 2005/01/15 09:00 [entrez]
PHST- 2009/04/30 00:00 [pmc-release]
AID - me.2004-0210 [pii]
AID - 10.1210/me.2004-0210 [doi]
PST - ppublish
SO  - Mol Endocrinol. 2005 Apr;19(4):863-78. doi: 10.1210/me.2004-0210. Epub 2005 Jan 
      13.