PMID- 10598588
OWN - NLM
STAT- MEDLINE
DCOM- 20000110
LR  - 20231213
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 13
IP  - 12
DP  - 1999 Dec
TI  - Constitutive activation of transcription and binding of coactivator by 
      estrogen-related receptors 1 and 2.
PG  - 2151-62
AB  - In this report, we demonstrate that, in contrast to most previously characterized 
      nuclear receptors, hERR1 and hERR2 (human estrogen receptor-related protein 1 and 
      -2) are constitutive activators of the classic estrogen response element (ERE) as 
      well as the palindromic thyroid hormone response element (TRE(pal)) but not the 
      glucocorticoid response element (GRE). This intrinsically activated state of 
      hERR1 and hERR2 resides in the ligand-binding domains of the two genes and is 
      transferable to a heterologous receptor. In addition, we show that members of the 
      p160 family of nuclear receptor coactivators, ACTR (activator of thyroid and 
      retinoic acid receptors), GRIP1 (glucocorticoid receptor interacting protein 1), 
      and SRC-1 (steroid receptor coactivator 1), potentiate the transcriptional 
      activity by hERR1 and hERR2 in mammalian cells, and that both orphan receptors 
      bind the coactivators in a ligand-independent manner. Together, these results 
      suggest that hERR1 and hERR2 activate gene transcription through a mechanism 
      different from most of the previously characterized steroid hormone receptors.
FAU - Xie, W
AU  - Xie W
AD  - Howard Hughes Medical Institute, Gene Expression Laboratory, The Salk Institute 
      for Biological Studies, La Jolla, California 92037, USA.
FAU - Hong, H
AU  - Hong H
FAU - Yang, N N
AU  - Yang NN
FAU - Lin, R J
AU  - Lin RJ
FAU - Simon, C M
AU  - Simon CM
FAU - Stallcup, M R
AU  - Stallcup MR
FAU - Evans, R M
AU  - Evans RM
LA  - eng
GR  - DK-43093/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (ESRRB protein, human)
RN  - 0 (Estrogens)
RN  - 0 (NCOA2 protein, human)
RN  - 0 (Nuclear Receptor Coactivator 2)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Estrogen)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Thyroid Hormones)
RN  - 0 (Transcription Factors)
RN  - EC 2.3.1.- (Acetyltransferases)
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)
SB  - IM
MH  - Acetyltransferases/metabolism/pharmacology
MH  - Cell Line
MH  - Drug Synergism
MH  - Estrogens/pharmacology
MH  - HeLa Cells
MH  - Histone Acetyltransferases
MH  - Humans
MH  - Nuclear Receptor Coactivator 1
MH  - Nuclear Receptor Coactivator 2
MH  - Receptors, Cytoplasmic and Nuclear/genetics/*metabolism
MH  - Receptors, Estrogen/*metabolism
MH  - Response Elements
MH  - *Saccharomyces cerevisiae Proteins
MH  - Thyroid Hormones/pharmacology
MH  - Transcription Factors/*metabolism/*pharmacology
MH  - *Transcription, Genetic
MH  - ERRalpha Estrogen-Related Receptor
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1210/mend.13.12.0381 [doi]
PST - ppublish
SO  - Mol Endocrinol. 1999 Dec;13(12):2151-62. doi: 10.1210/mend.13.12.0381.