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Retinoic acid receptor RXR-alpha

Definition:

Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription. The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation. Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA. The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells. Acts as an enhancer of RARA binding to RARE DNA element. May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1. Promotes myelin debris phagocytosis and remyelination by macrophages. Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes. Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence.

References:

[1]. R A Heyman, et al. 9-cis retinoic acid is a high affinity ligand for the retinoid X receptor. Cell. 1992 Jan 24;68(2):397-406. [Content Brief]

[2]. Feng Ma, et al. Retinoid X receptor α attenuates host antiviral response by suppressing type I interferon. Nat Commun. 2014 Nov 24;5:5494. [Content Brief]

[3]. Xingjie Ma, et al. The nuclear receptor RXRA controls cellular senescence by regulating calcium signaling. Aging Cell. 2018 Dec;17(6):e12831. [Content Brief]

[4]. David G Washburn, et al. Synthesis and SAR of potent LXR agonists containing an indole pharmacophore. Bioorg Med Chem Lett. 2009 Feb 15;19(4):1097-100. [Content Brief]

[5]. Wen-Xiu Zhao, et al. Orphan receptor TR3 attenuates the p300-induced acetylation of retinoid X receptor-alpha. Mol Endocrinol. 2007 Dec;21(12):2877-89. [Content Brief]

[6]. Vikas Chandra, et al. The quaternary architecture of RARβ-RXRα heterodimer facilitates domain-domain signal transmission. Nat Commun. 2017 Oct 11;8(1):868. [Content Brief]

[7]. Kirsten Prüfer, et al. Retinoid X receptor dominates the nuclear import and export of the unliganded vitamin D receptor. Mol Endocrinol. 2002 Aug;16(8):1738-51. [Content Brief]

[8]. Muktha S Natrajan, et al. Retinoid X receptor activation reverses age-related deficiencies in myelin debris phagocytosis and remyelination. Brain. 2015 Dec;138(Pt 12):3581-97. [Content Brief]

[9]. Takeya Tsutsumi, et al. Interaction of hepatitis C virus core protein with retinoid X receptor alpha modulates its transcriptional activity. Hepatology. 2002 Apr;35(4):937-46. [Content Brief]

[10]. Michael C Jaye, et al. Discovery of substituted maleimides as liver X receptor agonists and determination of a ligand-bound crystal structure. J Med Chem. 2005 Aug 25;48(17):5419-22. [Content Brief]

[11]. H Chen, et al. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [Content Brief]

[12]. Xihua Cao, et al. Retinoid X receptor regulates Nur77/TR3-dependent apoptosis [corrected] by modulating its nuclear export and mitochondrial targeting. Mol Cell Biol. 2004 Nov;24(22):9705-25. [Content Brief]

[13]. Esther Y Chao, et al. Structure-guided design of N-phenyl tertiary amines as transrepression-selective liver X receptor modulators with anti-inflammatory activity. J Med Chem. 2008 Sep 25;51(18):5758-65. [Content Brief]

[14]. Nadine C Santos, et al. Activity of retinoic acid receptor-alpha is directly regulated at its protein kinase A sites in response to follicle-stimulating hormone signaling. Endocrinology. 2010 May;151(5):2361-72. [Content Brief]

[15]. Ding-Yu Lee, et al. MicroRNA-10a is crucial for endothelial response to different flow patterns via interaction of retinoid acid receptors and histone deacetylases. Proc Natl Acad Sci U S A. 2017 Feb 21;114(8):2072-2077. [Content Brief]

[16]. S Harish, et al. Serine 27, a human retinoid X receptor alpha residue, phosphorylated by protein kinase A is essential for cyclicAMP-mediated downregulation of RXRalpha function. Biochem Biophys Res Commun. 2000 Dec 29;279(3):853-7. [Content Brief]

[17]. A Gorla-Bajszczak, et al. Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR. Mol Cell Endocrinol. 1999 Jan 25;147(1-2):37-47. [Content Brief]

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