PMID- 1331778
OWN - NLM
STAT- MEDLINE
DCOM- 19921221
LR  - 20081121
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 6
IP  - 9
DP  - 1992 Sep
TI  - Heterodimerization among thyroid hormone receptor, retinoic acid receptor, 
      retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, 
      and an endogenous liver protein.
PG  - 1468-78
AB  - Thyroid hormone receptor (TR) binds to DNA as a monomer, homodimer, and 
      heterodimer with nuclear proteins. We have confirmed that the TR can 
      heterodimerize with retinoid X receptors (RXRs)-alpha and -beta, and have found 
      that another member of the nuclear receptor superfamily, chicken ovalbumin 
      upstream promoter transcription factor (COUP-TF), also formed heterodimers with 
      the TR in the context of binding to a palindromic thyroid hormone-responsive 
      element (TREp). The interaction between COUP-TF and the TR was confirmed using 
      specific antibodies which supershifted the COUP-TF/TR DNA complexes. The complex 
      between the TR and the major TR heterodimerization partner in liver was 
      unaffected by antibodies to COUP-TF and RXR beta, but was supershifted by an 
      anti-RXR alpha antibody, indicating that the liver protein is highly related to 
      RXR alpha. Indeed, the TR/RXR and TR/liver protein heterodimers contact the same 
      guanidine residues in TREp. The retinoic acid receptor (RAR) also heterodimerized 
      with COUP-TF as well as with RXR alpha, RXR beta, and the TR heterodimerization 
      partner in liver. In contrast to its ability to heterodimerize with the TR and 
      RAR, we did not detect heterodimers between COUP-TF and either RXR alpha, RXR 
      beta, or the liver nuclear protein in the context of binding to the TREp. These 
      results show that the major TR heterodimerization partner in liver is highly 
      related to RXR alpha, but that other nuclear receptors such as COUP-TF can 
      heterodimerize with the TR and RAR, suggesting that selective protein-protein 
      interactions may be involved in the tissue and target gene specificities of 
      hormone action.
FAU - Berrodin, T J
AU  - Berrodin TJ
AD  - Department of Medicine, University of Pennsylvania School of Medicine, 
      Philadelphia 19104.
FAU - Marks, M S
AU  - Marks MS
FAU - Ozato, K
AU  - Ozato K
FAU - Linney, E
AU  - Linney E
FAU - Lazar, M A
AU  - Lazar MA
LA  - eng
GR  - 1RO1-DK-43806-01/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 (COUP Transcription Factor I)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - COUP Transcription Factor I
MH  - Carrier Proteins/*metabolism
MH  - DNA/metabolism
MH  - DNA-Binding Proteins/*metabolism
MH  - Liver/*chemistry
MH  - Nuclear Proteins/*metabolism
MH  - Protein Binding
MH  - Protein Conformation
MH  - *Protein Multimerization
MH  - Receptors, Cell Surface/*metabolism
MH  - Receptors, Retinoic Acid
MH  - Receptors, Thyroid Hormone/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Regulatory Sequences, Nucleic Acid
MH  - Retinoid X Receptors
MH  - Transcription Factors/*metabolism
EDAT- 1992/09/01 00:00
MHDA- 1992/09/01 00:01
CRDT- 1992/09/01 00:00
PHST- 1992/09/01 00:00 [pubmed]
PHST- 1992/09/01 00:01 [medline]
PHST- 1992/09/01 00:00 [entrez]
AID - 10.1210/mend.6.9.1331778 [doi]
PST - ppublish
SO  - Mol Endocrinol. 1992 Sep;6(9):1468-78. doi: 10.1210/mend.6.9.1331778.