Retinoid X receptor gamma

Wikipedia on Answers.com:

Retinoid X receptor gamma

Top

Home > Library > Miscellaneous > Wikipedia

Retinoid X receptor, gamma

Crystallographic structure of the DNA-binding domain of the Retinoid X receptor, gamma. PDB rendering based on 1by4.

Available structures

PDB

Ortholog search: PDBe, RCSB

List of PDB id codes
2GL8

Identifiers

Symbols

RXRG; NR2B3; RXRC

External IDs

OMIM: 180247 MGI: 98216 HomoloGene: 21373 IUPHAR: NR2B3 GeneCards: RXRG Gene

Gene Ontology
Molecular function	• sequence-specific DNA binding transcription factor activity • steroid hormone receptor activity • receptor activity • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity • 9-cis retinoic acid receptor activity • steroid binding • zinc ion binding • sequence-specific DNA binding • metal ion binding
Cellular component	• nucleus • nucleoplasm
Biological process	• peripheral nervous system development • heart development • skeletal muscle tissue development • gene expression • response to organic cyclic compound • neuron differentiation • response to retinoic acid • cellular response to hormone stimulus • positive regulation of transcription from RNA polymerase II promoter • retinoic acid receptor signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
165.37 – 165.41 Mb

Chr 1:
169.53 – 169.57 Mb

PubMed search

[1]

[2]

Retinoic acid receptor gamma (RXR-gamma), also known as NR2B3 (nuclear receptor subfamily 2, group B, member 3) is a nuclear receptor that in humans is encoded by the RXRG gene.^[1]^[2]

This gene encodes a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the antiproliferative effects of retinoic acid (RA). This receptor forms heterodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. This gene is expressed at significantly lower levels in non-small cell lung cancer cells. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[2]

Contents

1 See also
2 Interactions
3 References
4 Further reading

Interactions

Retinoid X receptor gamma has been shown to interact with ITGB3BP.^[3]

References

^ Almasan A, Mangelsdorf DJ, Ong ES, Wahl GM, Evans RM (April 1994). "Chromosomal localization of the human retinoid X receptors". Genomics 20 (3): 397–403. doi:10.1006/geno.1994.1193. PMID 8034312.
^ ^a ^b "Entrez Gene: RXRG retinoid X receptor, gamma". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6258.
^ Li, D; Wang F, Samuels H H (Dec. 2001). "Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation". Mol. Cell. Biol. (United States) 21 (24): 8371–84. doi:10.1128/MCB.21.24.8371-8384.2001. ISSN 0270-7306. PMC 100002. PMID 11713274. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=100002.

Szanto A, Narkar V, Shen Q, et al. (2005). "Retinoid X receptors: X-ploring their (patho)physiological functions.". Cell Death Differ. 11 Suppl 2: S126–43. doi:10.1038/sj.cdd.4401533. PMID 15608692.
Leid M, Kastner P, Lyons R, et al. (1992). "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently.". Cell 68 (2): 377–95. doi:10.1016/0092-8674(92)90478-U. PMID 1310259.
Mangelsdorf DJ, Borgmeyer U, Heyman RA, et al. (1992). "Characterization of three RXR genes that mediate the action of 9-cis retinoic acid.". Genes Dev. 6 (3): 329–44. doi:10.1101/gad.6.3.329. PMID 1312497.
Nagata T, Weiss EH, Abe K, et al. (1995). "Physical mapping of the retinoid X receptor B gene in mouse and human.". Immunogenetics 41 (2–3): 83–90. doi:10.1007/BF00182317. PMID 7806300.
Muscat GE, Mynett-Johnson L, Dowhan D, et al. (1994). "Activation of myoD gene transcription by 3,5,3'-triiodo-L-thyronine: a direct role for the thyroid hormone and retinoid X receptors". Nucleic Acids Res. 22 (4): 583–91. doi:10.1093/nar/22.4.583. PMC 307847. PMID 8127707. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=307847.
Kamei Y, Xu L, Heinzel T, et al. (1996). "A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors". Cell 85 (3): 403–14. doi:10.1016/S0092-8674(00)81118-6. PMID 8616895.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Sanno N, Sugawara A, Teramoto A, et al. (1997). "Immunohistochemical expression of retinoid X receptor isoforms in human pituitaries and pituitary adenomas". Neuroendocrinology 65 (4): 299–306. doi:10.1159/000127188. PMID 9143002.
Reichrath J, Mittmann M, Kamradt J, Müller SM (1997). "Expression of retinoid-X receptors (-alpha,-beta,-gamma) and retinoic acid receptors (-alpha,-beta,-gamma) in normal human skin: an immunohistological evaluation". Histochem. J. 29 (2): 127–33. doi:10.1023/A:1026481205135. PMID 9147069.
Xu XC, Sozzi G, Lee JS, et al. (1997). "Suppression of retinoic acid receptor beta in non-small-cell lung cancer in vivo: implications for lung cancer development". J. Natl. Cancer Inst. 89 (9): 624–9. doi:10.1093/jnci/89.9.624. PMID 9150186.
Yusta B, Alarid ET, Gordon DF, et al. (1998). "The thyrotropin beta-subunit gene is repressed by thyroid hormone in a novel thyrotrope cell line, mouse T alphaT1 cells". Endocrinology 139 (11): 4476–82. doi:10.1210/en.139.11.4476. PMID 9794455.
Ito K, Suzuki T, Moriya T, et al. (2001). "Retinoid receptors in the human endometrium and its disorders: a possible modulator of 17 beta-hydroxysteroid dehydrogenase". J. Clin. Endocrinol. Metab. 86 (6): 2721–7. doi:10.1210/jc.86.6.2721. PMID 11397877.
Kim SW, Kim HJ, Jung DJ, et al. (2001). "Retinoid-dependent antagonism of serum response factor transactivation mediated by transcriptional coactivator proteins". Oncogene 20 (45): 6638–42. doi:10.1038/sj.onc.1204695. PMID 11641790.
Brabender J, Danenberg KD, Metzger R, et al. (2002). "The role of retinoid X receptor messenger RNA expression in curatively resected non-small cell lung cancer". Clin. Cancer Res. 8 (2): 438–43. PMID 11839661.
Wansa KD, Harris JM, Muscat GE (2002). "The activation function-1 domain of Nur77/NR4A1 mediates trans-activation, cell specificity, and coactivator recruitment". J. Biol. Chem. 277 (36): 33001–11. doi:10.1074/jbc.M203572200. PMID 12082103.
Wang Q, Fujii H, Knipp GT (2003). "Expression of PPAR and RXR isoforms in the developing rat and human term placentas". Placenta 23 (8–9): 661–71. doi:10.1053/plac.2002.0855. PMID 12361685.
Kimura Y, Suzuki T, Kaneko C, et al. (2003). "Retinoid receptors in the developing human lung". Clin. Sci. 103 (6): 613–21. PMID 12444914.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Alfaro JM, Fraile B, Lobo MV, et al. (2003). "Immunohistochemical detection of the retinoid X receptors alpha, beta, and gamma in human prostate". J. Androl. 24 (1): 113–9. PMID 12514092.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

PDB gallery

1by4: STRUCTURE AND MECHANISM OF THE HOMODIMERIC ASSEMBLY OF THE RXR ON DNA

1dsz: STRUCTURE OF THE RXR/RAR DNA-BINDING DOMAIN HETERODIMER IN COMPLEX WITH THE RETINOIC ACID RESPONSE ELEMENT DR1

1r0n: Crystal Structure of Heterodimeric Ecdsyone receptor DNA binding complex

1rxr: HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE

2gl8: Human Retinoic acid receptor RXR-gamma ligand-binding domain

2nll: RETINOID X RECEPTOR-THYROID HORMONE RECEPTOR DNA-BINDING DOMAIN HETERODIMER BOUND TO THYROID RESPONSE ELEMENT DNA

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) · AP-1 (c-Fos, FOSB, FOSL1, FOSL2, JDP2, c-Jun, JUNB, JUND) · BACH (1, 2) · BATF · BLZF1 · C/EBP (α, β, γ, δ, ε, ζ) · CREB (1, 3, L1) · CREM · DBP · DDIT3 · GABPA · HLF · MAF (B, F, G, K) · NFE (2, L1, L2, L3) · NFIL3 · NRL · NRF (1, 2, 3) · XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLHB2 · BMAL (ARNTL, ARNTL2) · CLOCK · EPAS1 · FIGLA · HAND (1, 2) · HES (5, 6) · HEY (1, 2, L) · HES1 · HIF (1A, 3A) · ID (1, 2, 3, 4) · LYL1 · MESP2 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) · Neurogenins (1, 2, 3) · NeuroD (1, 2) · NPAS (1, 2, 3) · OLIG (1, 2) · Pho4 · Scleraxis · SIM (1, 2) · TAL (1, 2) · Twist · USF1

(1.3) bHLH-ZIP	AP-4 · MAX · MITF · MNT · MLX · MXI1 · Myc · SREBP (1, 2)

(1.4) NF-1	NFI (A, B, C, X) · SMAD (R-SMAD (1, 2, 3, 5, 9) - I-SMAD (6, 7) - 4)

(1.5) RF-X	RFX (1, 2, 3, 4, 5, 6, ANK)

(1.6) Basic helix-span-helix (bHSH)	AP-2 (α, β, γ, δ, ε)

(2) Zinc finger DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) subfamily 3 (Steroid hormone (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ)) subfamily 4 NUR (NGFIB, NOR1, NURR1) · subfamily 5 (LRH-1, SF1) · subfamily 6 (GCNF) · subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) · MTA (1, 2, 3) · TRPS1

(2.3) Cys₂His₂	General transcription factors (TFIIA, TFIIB, TFIID, TFIIE (1, 2), TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2)) ATBF1 · BCL (6, 11A, 11B) · CTCF · E4F1 · EGR (1, 2, 3, 4) · ERV3 · GFI1 · GLI-Krüppel family (1, 2, 3, REST, S2, YY1) · HIC (1, 2) · HIVEP (1, 2, 3) · IKZF (1, 2, 3) · ILF (2, 3) · KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17) · MTF1 · MYT1 · OSR1 · PRDM9 · SALL (1, 2, 3, 4) · SP (1, 2, 4, 7, 8) · TSHZ3 · WT1 · Zbtb7 (7A, 7B) · ZBTB (11, 16, 17, 20, 32, 33, 40) · zinc finger (3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 300, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 644, 649, 655)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE · DIDO1 · GRLF1 · ING (1, 2, 4) · JARID (1A, 1B, 1C, 1D, 2) · JMJD1B

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX · CDX (1, 2) · CRX · CUTL1 · DBX (1, 2) · DLX (3, 4, 5) · EMX (1, 2) · EN (1, 2) · FHL (1, 2, 3) · HESX1 · HHEX · HLX · Homeobox (A1, A2, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C12, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) · HOPX · IRX (1, 2, 3, 4, 5, 6, MKX) · LMX (1A, 1B) · MEIS (1, 2) · MEOX2 · MNX1 · MSX (1, 2) · NANOG · NKX (2-1, 2-2, 2-3, 2-5, 3-1, 3-2, 6-1, 6-2) · NOBOX · PBX (1, 2, 3) · PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) · PHOX (2A, 2B) · PITX (1, 2, 3) · POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX (1, 2) · PDX1 · SATB2 · SHOX2 · VAX1 · ZEB (1, 2)

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) · FOX proteins (A1, A2, A3, C1, C2, D3, D4, E1, E3, F1, G1, H1, I1, J1, J2, K1, K2, L2, M1, N1, N3, O1, O3, O4, P1, P2, P3, P4)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (2, 4, 5) · EGF · ELK (1, 3, 4) · ERF · ETS (1, 2, ERG, SPIB) · ETV (1, 4, 5, 6) · FLI1 · Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) · MYB · MYBL2

(3.6) TEA domain	transcriptional enhancer factor (1, 2, 3, 4)

(4) β-Scaffold factors with minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) · NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53 · TBX (1, 2, 3, 5, 19, 21, 22, Brachyury, TBR1, TBR2) · TP63

(4.4) MADS box	Mef2 (A, B, C, D) · SRF

(4.6) TATA binding proteins	TBP · TBPL1

(4.7) High-mobility group	BBX · HMGB (1, 2, 3, 4) · HMGN (1, 2, 3, 4) · HNF (1A, 1B) · LEF1 · SOX (1, 2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21) · SRY · SSRP1 · TCF (3, 4) · TOX (1, 2, 3, 4)

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) · HBP1

(0.3) Pocket domain	Rb · RBL1 · RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 · EREBP · B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) · CAP · IFI (16, 35) · MLL (2, 3, T1) · MNDA · NFY (A, B, C) · Rho/Sigma

see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

This article on a gene on chromosome 1 is a stub. You can help Wikipedia by expanding it.

This entry is from Wikipedia, the leading user-contributed encyclopedia. It may not have been reviewed by professional editors (see full disclaimer)

Donate to Wikimedia

Help us answer these

If x is a gamma RV what is the distribution of x squared?

What are gamma-amino-butyric acid receptors?

Why are gamma rays and x rays ionising?

How do satellites observe gamma and x-rays?

Post a question - any question - to the WikiAnswers community:

Copyrights:

Cite

Wikipedia on Answers.com This article is licensed under the Creative Commons Attribution/Share-Alike License. It uses material from the Wikipedia article Retinoid X receptor gamma. Read