PMID- 9584188
OWN - NLM
STAT- MEDLINE
DCOM- 19980617
LR  - 20210526
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 18
IP  - 6
DP  - 1998 Jun
TI  - Transactivation by retinoid X receptor-peroxisome proliferator-activated receptor 
      gamma (PPARgamma) heterodimers: intermolecular synergy requires only the 
      PPARgamma hormone-dependent activation function.
PG  - 3483-94
AB  - The ability of DNA sequence-specific transcription factors to synergistically 
      activate transcription is a common property of genes transcribed by RNA 
      polymerase II. The present work characterizes a unique form of intermolecular 
      transcriptional synergy between two members of the nuclear hormone receptor 
      superfamily. Heterodimers formed between peroxisome proliferator-activated 
      receptor gamma (PPARgamma), an adipocyte-enriched member of the superfamily 
      required for adipogenesis, and retinoid X receptors (RXRs) can activate 
      transcription in response to ligands specific for either subunit of the dimer. 
      Simultaneous treatment with ligands specific for both PPARgamma and RXR has a 
      synergistic effect on the transactivation of reporter genes and on adipocyte 
      differentiation in cultured cells. Mutation of the PPARgamma hormone-dependent 
      activation domain (named tauc or AF-2) inhibits the ability of RXR-PPARgamma 
      heterodimers to respond to ligands specific for either subunit. In contrast, the 
      ability of RXR- and PPARgamma-specific ligands to synergize does not require the 
      hormone-dependent activation domain of RXR. The results of in vitro and in vivo 
      experiments indicate that binding of ligands to RXR alters the conformation of 
      the dimerization partner, PPARgamma, and modulates the activity of the 
      heterodimer in a manner independent of the RXR hormone-dependent activation 
      domain.
FAU - Schulman, I G
AU  - Schulman IG
AD  - Department of Retinoid Research, Ligand Pharmaceuticals, San Diego, California 
      92121, USA. ischulman@ligand.com
FAU - Shao, G
AU  - Shao G
FAU - Heyman, R A
AU  - Heyman RA
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Ligands)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
RN  - EC 2.3.1.48 (Ncoa1 protein, mouse)
RN  - EC 2.3.1.48 (Nuclear Receptor Coactivator 1)
SB  - IM
MH  - 3T3 Cells
MH  - Adipocytes/cytology
MH  - Animals
MH  - Binding Sites
MH  - Cell Differentiation
MH  - DNA-Binding Proteins/*metabolism
MH  - Dimerization
MH  - Histone Acetyltransferases
MH  - Ligands
MH  - Macromolecular Substances
MH  - Mice
MH  - Microbodies/*metabolism
MH  - Nuclear Proteins/*metabolism
MH  - Nuclear Receptor Coactivator 1
MH  - Protein Conformation
MH  - Receptors, Cytoplasmic and Nuclear/*metabolism
MH  - Receptors, Retinoic Acid/*metabolism
MH  - Retinoid X Receptors
MH  - Transcription Factors/*metabolism
MH  - *Transcriptional Activation
PMC - PMC108929
EDAT- 1998/06/20 00:00
MHDA- 1998/06/20 00:01
PMCR- 1998/06/01
CRDT- 1998/06/20 00:00
PHST- 1998/06/20 00:00 [pubmed]
PHST- 1998/06/20 00:01 [medline]
PHST- 1998/06/20 00:00 [entrez]
PHST- 1998/06/01 00:00 [pmc-release]
AID - 1634 [pii]
AID - 10.1128/MCB.18.6.3483 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1998 Jun;18(6):3483-94. doi: 10.1128/MCB.18.6.3483.