PMID- 9514150
OWN - NLM
STAT- MEDLINE
DCOM- 19980514
LR  - 20061115
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 12
IP  - 3
DP  - 1998 Mar
TI  - Identification of critical residues for heterodimerization within the 
      ligand-binding domain of retinoid X receptor.
PG  - 325-32
AB  - Nuclear receptors regulate transcription by binding to specific DNA response 
      elements as homodimers or heterodimers with the retinoid X receptors (RXRs). The 
      identity box (I-box), a 40-amino acid region within the ligand-binding domains of 
      RXRs and other nuclear receptors, was recently shown to determine identity in the 
      heterodimeric interactions. Here, we dissected this region in the yeast 
      two-hybrid system by analyzing a series of chimeric receptors between human 
      RXRalpha and rat hepatocyte nuclear factor 4 (HNF4), a distinct member of the 
      nuclear receptor superfamily that prefers homodimerization. We found that the 
      C-terminal 11-amino acid region of the RXR I-box was sufficient to direct 
      chimeric receptors based on the HNF4 ligand-binding domain to heterodimerize with 
      retinoic acid receptors or thyroid hormone receptors. Furthermore, we identified 
      the hRXRalpha amino acids A416 and R421 of the 11-amino acid subregion as most 
      critical determinants of heterodimeric interactions; i.e. mutant HNF4s 
      incorporating only the hRXRalpha A416 or R421 heterodimerized with retinoic acid 
      receptor.
FAU - Lee, S K
AU  - Lee SK
AD  - College of Pharmacy, Chonnam National University, Kwangju, Korea.
FAU - Na, S Y
AU  - Na SY
FAU - Kim, H J
AU  - Kim HJ
FAU - Soh, J
AU  - Soh J
FAU - Choi, H S
AU  - Choi HS
FAU - Lee, J W
AU  - Lee JW
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (Bacterial Proteins)
RN  - 0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Hepatocyte Nuclear Factor 4)
RN  - 0 (LexA protein, Bacteria)
RN  - 0 (MLX protein, human)
RN  - 0 (Phosphoproteins)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
RN  - EC 3.4.21.- (Serine Endopeptidases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bacterial Proteins/genetics/metabolism
MH  - Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
MH  - Binding Sites
MH  - *DNA-Binding Proteins
MH  - Dimerization
MH  - Hepatocyte Nuclear Factor 4
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Phosphoproteins/chemistry/genetics/*metabolism
MH  - Rats
MH  - Receptors, Retinoic Acid/*chemistry/genetics/*metabolism
MH  - Recombinant Proteins/genetics/metabolism
MH  - Retinoid X Receptors
MH  - Serine Endopeptidases/genetics/metabolism
MH  - Transcription Factors/*chemistry/genetics/*metabolism
MH  - Yeasts/genetics
EDAT- 1998/03/26 00:00
MHDA- 1998/03/26 00:01
CRDT- 1998/03/26 00:00
PHST- 1998/03/26 00:00 [pubmed]
PHST- 1998/03/26 00:01 [medline]
PHST- 1998/03/26 00:00 [entrez]
AID - 10.1210/mend.12.3.0072 [doi]
PST - ppublish
SO  - Mol Endocrinol. 1998 Mar;12(3):325-32. doi: 10.1210/mend.12.3.0072.