ArticleMolecular and cellular biology1995
Mouse retinoid X receptor contains a separable ligand-binding and transactivation domain in its E region.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 95 citations in OpenAlex.
- Ligand-Dependent Corepressor (LCoR) Is a Rexinoid-Inhibited Peroxisome Proliferator-Activated Receptor γ-Retinoid X Receptor α Coactivator.Molecular and cellular biology · 2018Article
- The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression.Molecular and cellular biology · 2000Article
- NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors.Molecular and cellular biology · 1999Article
- A novel role for helix 12 of retinoid X receptor in regulating repression.Molecular and cellular biology · 1999Article
- The histone acetylase PCAF is a nuclear receptor coactivator.Genes & development · 1998Article
- Nuclear receptor DAX-1 recruits nuclear receptor corepressor N-CoR to steroidogenic factor 1.Molecular and cellular biology · 1998Article
- Mutations in the conserved C-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity.Molecular and cellular biology · 1997Article
- tau4/tau c/AF-2 of the thyroid hormone receptor relieves silencing of the retinoic acid receptor silencer core independent of both tau4 activation function and full dissociation of corepressors.Molecular and cellular biology · 1997Article
- Activation of the orphan receptor RIP14 by retinoids.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Nuclear receptor steroidogenic factor 1 directs embryonic stem cells toward the steroidogenic lineage.Molecular and cellular biology · 1997Article
- Heterodimeric interaction between retinoid X receptor alpha and orphan nuclear receptor OR1 reveals dimerization-induced activation as a novel mechanism of nuclear receptor activation.Molecular and cellular biology · 1997Article
- Retinoid X receptor:vitamin D3 receptor heterodimers promote stable preinitiation complex formation and direct 1,25-dihydroxyvitamin D3-dependent cell-free transcription.Molecular and cellular biology · 1997Article
- Retinoid X receptor (RXR) within the RXR-retinoic acid receptor heterodimer binds its ligand and enhances retinoid-dependent gene expression.Molecular and cellular biology · 1997Article
- A natural transactivation mutation in the thyroid hormone beta receptor: impaired interaction with putative transcriptional mediators.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- The extreme C terminus of progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors.The EMBO journal · 1996Article
- Activation and repression by nuclear hormone receptors: hormone modulates an equilibrium between active and repressive states.Molecular and cellular biology · 1996Article
- Molecular mechanisms of COUP-TF-mediated transcriptional repression: evidence for transrepression and active repression.Molecular and cellular biology · 1996Article
- The vitamin D(3) receptor in the context of the nuclear receptor superfamily : The central role of the retinoid X receptor.Endocrine · 1996Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Steroid, thyroid, and retinoid hormones exert their biological functions by interacting with their cognate nuclear receptors. Upon binding receptors, hormones induce a protease-resistant structural change in the receptor ligand-binding domain and subsequently activate the receptors. Utilizing partial proteolysis, we have been able to delineate a region in the mouse retinoid X receptor beta (mRXR beta) required for ligand binding. A separable activation domain within the mRXR beta E region has been identified. The activation domain, which is 21 amino acids in length, is located at the extreme C terminus of mRXR beta. This domain is not required for ligand binding since removal of this sequence neither eliminates the ligand-induced, protease-resistant conformational change nor alters the ligand-enhanced DNA binding. Furthermore, deletion of this activation domain converts the receptor into a transcriptional silencer. Finally, a further truncation of 9 amino acids (for a total of 30 amino acids) from the C terminus results in a mutant which does not undergo the protease-resistant conformational change and cannot bind DNA as a homodimer. Nevertheless, this mutant is still able to form a heterodimer with the thyroid hormone receptor. Therefore, homodimerization and heterodimerization can be distinguished by this nine-amino-acid sequence.
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