PMID- 9841885
OWN - NLM
STAT- MEDLINE
DCOM- 19990225
LR  - 20190501
IS  - 0264-6021 (Print)
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 336 ( Pt 3)
IP  - Pt 3
DP  - 1998 Dec 15
TI  - Differential modulation of transcriptional activity of oestrogen receptors by 
      direct protein-protein interactions with retinoid receptors.
PG  - 711-7
AB  - Control of oestradiol-responsive gene regulation by oestrogen receptors (ERs) may 
      involve complex cross-talk with retinoic acid receptors (RARs) and retinoid X 
      receptors (RXRs). Recently, we have shown that ERalpha directly interacts with 
      RARalpha and RXRalpha through their ligand binding domains (LBDs). In the present 
      work, we extend these results by showing that ERbeta binds similarly to RARalpha 
      and RXRalpha but not to the glucocorticoid receptor, as demonstrated by the yeast 
      two-hybrid tests and glutathione S-transferase pull-down assays. These direct 
      interactions were also demonstrated in gel-shift assays, in which the oestrogen 
      response element (ERE) binding by ERalpha was enhanced by the RXRalpha LBD but 
      was abolished by the RARalpha LBD. In addition, we showed that RARalpha and 
      RXRalpha bound the ERE as efficiently as ERalpha, suggesting that competition for 
      DNA binding may affect the transactivation function of the ER. In transient 
      transfection experiments, co-expression of RARalpha or RXRalpha, along with 
      ERalpha or ERbeta, revealed differential modulation of the ERE-dependent 
      transactivation, which was distinct from the results when each receptor alone was 
      co-transfected. Importantly, when the LBD of RARalpha was co-expressed with 
      ERalpha, transactivation of ERalpha on the ERE was repressed as efficiently as 
      when wild-type RARalpha was co-expressed. Furthermore, liganded RARalpha or 
      unliganded RXRalpha enhanced the ERalpha transactivation, suggesting the 
      formation of transcriptionally active heterodimer complexes between the ER and 
      retinoid receptors. Taken together, these results suggest that direct 
      protein-protein interactions may play major roles in the determination of the 
      biological consequences of cross-talk between ERs and RARalpha or RXRalpha.
FAU - Song, M R
AU  - Song MR
AD  - Department of Microbiology, Yonsei University College of Medicine, Seoul, 120-752 
      Korea.
FAU - Lee, S K
AU  - Lee SK
FAU - Seo, Y W
AU  - Seo YW
FAU - Choi, H S
AU  - Choi HS
FAU - Lee, J W
AU  - Lee JW
FAU - Lee, M O
AU  - Lee MO
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Receptors, Estrogen)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Culture Techniques
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Humans
MH  - Protein Binding
MH  - Receptors, Estrogen/*genetics/*metabolism
MH  - Receptors, Retinoic Acid/*metabolism
MH  - Retinoid X Receptors
MH  - Transcription Factors/*metabolism
MH  - *Transcriptional Activation
MH  - Transfection
MH  - Tumor Cells, Cultured
PMC - PMC1219924
EDAT- 1998/12/08 00:00
MHDA- 1998/12/08 00:01
PMCR- 1999/06/15
CRDT- 1998/12/08 00:00
PHST- 1998/12/08 00:00 [pubmed]
PHST- 1998/12/08 00:01 [medline]
PHST- 1998/12/08 00:00 [entrez]
PHST- 1999/06/15 00:00 [pmc-release]
AID - 10.1042/bj3360711 [doi]
PST - ppublish
SO  - Biochem J. 1998 Dec 15;336 ( Pt 3)(Pt 3):711-7. doi: 10.1042/bj3360711.