PMID- 10523643
OWN - NLM
STAT- MEDLINE
DCOM- 19991124
LR  - 20220310
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 11
DP  - 1999 Nov
TI  - Heterodimerization between members of the Nur subfamily of orphan nuclear 
      receptors as a novel mechanism for gene activation.
PG  - 7549-57
AB  - We have recently shown that the orphan nuclear receptor Nur77 (NGFI-B) is most 
      active in transcription when it is interacting with a cognate DNA sequence as a 
      homodimer. Further, we have shown that the target for Nur77 dimers, the Nur 
      response element (NurRE), is responsive to physiological stimuli in both 
      endocrine and lymphoid cells, whereas other DNA targets of Nur77 action are not. 
      The Nur77 subfamily also includes two related receptors, Nur-related factor 1 
      (Nurr1) and neuron-derived orphan receptor 1 (NOR-1). Often, more than one member 
      of this subfamily is induced in response to extracellular signals. We now show 
      that Nur77 and Nurr1 form heterodimers in vitro in the presence or absence of 
      NurRE, and we have documented interactions between these proteins in vivo by 
      using a two-hybrid system in mammalian cells. These heterodimers synergistically 
      enhance transcription from NurRE reporters in comparison to that seen with 
      homodimers. The naturally occurring NurRE from the pro-opiomelanocortin gene 
      preferentially binds and activates transcription in the presence of Nur77 homo- 
      or heterodimers, while a consensus NurRE sequence does not show this preference. 
      Taken together, the data indicate that members of the Nur77 subfamily are most 
      potent as heterodimers and that different dimers exhibit target sequence 
      preference. Thus, we propose that a combinatorial code relying on specific NurRE 
      sequences might be responsible for the activation of subsets of target genes by 
      one of the members of the Nur77 subfamily of transcription factors.
FAU - Maira, M
AU  - Maira M
AD  - Laboratoire de Genetique Moleculaire, Institut de Recherches Cliniques de 
      Montreal, Montreal, Quebec H2W 1R7, Canada.
FAU - Martens, C
AU  - Martens C
FAU - Philips, A
AU  - Philips A
FAU - Drouin, J
AU  - Drouin J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (NR4A1 protein, human)
RN  - 0 (NR4A2 protein, human)
RN  - 0 (NR4A3 protein, human)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Nuclear Receptor Subfamily 4, Group A, Member 1)
RN  - 0 (Nuclear Receptor Subfamily 4, Group A, Member 2)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Steroid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Transcription Factors)
RN  - 66796-54-1 (Pro-Opiomelanocortin)
RN  - 9015-71-8 (Corticotropin-Releasing Hormone)
SB  - IM
MH  - Corticotropin-Releasing Hormone/pharmacology
MH  - DNA-Binding Proteins/*metabolism
MH  - Dimerization
MH  - Genes, Reporter
MH  - Models, Genetic
MH  - Nerve Tissue Proteins/metabolism
MH  - Nuclear Receptor Subfamily 4, Group A, Member 1
MH  - Nuclear Receptor Subfamily 4, Group A, Member 2
MH  - Pro-Opiomelanocortin/*genetics
MH  - Protein Binding
MH  - Receptors, Cytoplasmic and Nuclear/*metabolism
MH  - Receptors, Steroid
MH  - Receptors, Thyroid Hormone
MH  - *Response Elements
MH  - Transcription Factors/*metabolism
MH  - *Transcriptional Activation
MH  - Two-Hybrid System Techniques
PMC - PMC84765
EDAT- 1999/10/19 00:00
MHDA- 1999/10/19 00:01
PMCR- 1999/11/01
CRDT- 1999/10/19 00:00
PHST- 1999/10/19 00:00 [pubmed]
PHST- 1999/10/19 00:01 [medline]
PHST- 1999/10/19 00:00 [entrez]
PHST- 1999/11/01 00:00 [pmc-release]
AID - 0291 [pii]
AID - 10.1128/MCB.19.11.7549 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Nov;19(11):7549-57. doi: 10.1128/MCB.19.11.7549.