Wikipedia

Receptor X retinoide alfa

gen de la especie Homo sapiens

El receptor X retinoide alfa (RXRA), también conocido como NR2B1 (de sus siglas en inglés "nuclear receptor subfamily 2, group B, member 1"), es un receptor nuclear codificado, en humanos, por el gen rxrA.[1]​

Receptor X retinoide alfa

Estructura tridimensional del receptor RXRA.
Estructuras disponibles
PDB

Buscar ortólogos: PDBe, RCSB

 Lista de códigos PDB
1by4
Identificadores
Símbolo RXRA (HGNC: 10477)
Identificadores
externos
Locus Cr. 9 q34
Ortólogos
Especies
Humano Ratón
Entrez
6256
UniProt
P19793 n/a
RefSeq
(ARNm)
NM_002957 n/a
[editar datos en Wikidata]

Los receptores X retinoides (RXRs) y los receptores de ácido retinoico (RARs) son receptores nucleares que actúan como intermediarios de los efectos biológicos de los retinoides en la activación del gen que codifica las proteínas implicadas en la síntesis de ácido retinoico. Estos receptores ejercen su acción mediante la unión, como homodímeros o como heterodímeros, a secuencias específicas en los promotores de los genes diana, y la regulación de su transcripción. La proteína RXRA es un miembro de la superfamilia de factores de transcripción de receptores de hormonas tiroideas y esteroideas.[2]​

Interacciones editar

El receptor X retinoide alfa ha demostrado ser capaz de interaccionar con:

Véase también editar

Referencias editar

  1. ↑ Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (mayo de 1990). «Nuclear receptor that identifies a novel retinoic acid response pathway». Nature 345 (6272): 224-9. PMID 2159111. doi:10.1038/345224a0. 
  2. ↑ «Entrez Gene: RXRA retinoid X receptor, alpha». 
  3. ↑ Na, S Y; Kim H J, Lee S K, Choi H S, Na D S, Lee M O, Chung M, Moore D D, Lee J W (Feb. de 1998). «IkappaBbeta interacts with the retinoid X receptor and inhibits retinoid-dependent transactivation in lipopolysaccharide-treated cells». J. Biol. Chem. (UNITED STATES) 273 (6): 3212-5. ISSN 0021-9258. PMID 9452433. 
  4. ↑ a b McNamara, P; Seo S B, Rudic R D, Sehgal A, Chakravarti D, FitzGerald G A (Jun. de 2001). «Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock». Cell (United States) 105 (7): 877-89. ISSN 0092-8674. PMID 11439184. 
  5. ↑ Thénot, S; Henriquet C, Rochefort H, Cavaillès V (mayo. de 1997). «Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1». J. Biol. Chem. (UNITED STATES) 272 (18): 12062-8. ISSN 0021-9258. PMID 9115274. 
  6. ↑ a b c Lee, Wen-yi; Noy Noa (Feb. de 2002). «Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain». Biochemistry (United States) 41 (8): 2500-8. ISSN 0006-2960. PMID 11851396. 
  7. ↑ a b Zhang, C; Baudino T A, Dowd D R, Tokumaru H, Wang W, MacDonald P N (Nov. de 2001). «Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription». J. Biol. Chem. (United States) 276 (44): 40614-20. ISSN 0021-9258. PMID 11514567. doi:10.1074/jbc.M106263200. 
  8. ↑ Lee, Y K; Dell H, Dowhan D H, Hadzopoulou-Cladaras M, Moore D D (Jan. de 2000). «The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression». Mol. Cell. Biol. (UNITED STATES) 20 (1): 187-95. ISSN 0270-7306. PMID 10594021. 
  9. ↑ Brendel, Carole; Schoonjans Kristina, Botrugno Oronza A, Treuter Eckardt, Auwerx Johan (Sep. de 2002). «The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity». Mol. Endocrinol. (United States) 16 (9): 2065-76. ISSN 0888-8809. PMID 12198243. 
  10. ↑ Préfontaine, G G; Walther R, Giffin W, Lemieux M E, Pope L, Haché R J (Sep. de 1999). «Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter». J. Biol. Chem. (UNITED STATES) 274 (38): 26713-9. ISSN 0021-9258. PMID 10480874. 
  11. ↑ Kakizawa, T; Miyamoto T, Ichikawa K, Kaneko A, Suzuki S, Hara M, Nagasawa T, Takeda T, Mori J i, Kumagai M, Hashizume K (Jul. de 1999). «Functional interaction between Oct-1 and retinoid X receptor». J. Biol. Chem. (UNITED STATES) 274 (27): 19103-8. ISSN 0021-9258. PMID 10383413. 
  12. ↑ Li, D; Desai-Yajnik V, Lo E, Schapira M, Abagyan R, Samuels H H (Oct. de 1999). «NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors». Mol. Cell. Biol. (UNITED STATES) 19 (10): 7191-202. ISSN 0270-7306. PMID 10490654. 
  13. ↑ Schulman, I G; Chakravarti D, Juguilon H, Romo A, Evans R M (Aug. de 1995). «Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 92 (18): 8288-92. ISSN 0027-8424. PMID 7667283. 
  14. ↑ Liu, B; Lee H Y, Weinzimer S A, Powell D R, Clifford J L, Kurie J M, Cohen P (Oct. de 2000). «Direct functional interactions between insulin-like growth factor-binding protein-3 and retinoid X receptor-alpha regulate transcriptional signaling and apoptosis». J. Biol. Chem. (UNITED STATES) 275 (43): 33607-13. ISSN 0021-9258. PMID 10874028. doi:10.1074/jbc.M002547200. 
  15. ↑ Chen, H; Lin R J, Schiltz R L, Chakravarti D, Nash A, Nagy L, Privalsky M L, Nakatani Y, Evans R M (Aug. de 1997). «Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300». Cell (UNITED STATES) 90 (3): 569-80. ISSN 0092-8674. PMID 9267036. 
  16. ↑ Farooqui, Mariya; Franco Peter J, Thompson Jim, Kagechika Hiroyuki, Chandraratna Roshantha A S, Banaszak Len, Wei Li-Na (Feb. de 2003). «Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity». Biochemistry (United States) 42 (4): 971-9. ISSN 0006-2960. PMID 12549917. doi:10.1021/bi020497k. 
  17. ↑ L'Horset, F; Dauvois S, Heery D M, Cavaillès V, Parker M G (Nov. de 1996). «RIP-140 interacts with multiple nuclear receptors by means of two distinct sites». Mol. Cell. Biol. (UNITED STATES) 16 (11): 6029-36. ISSN 0270-7306. PMID 8887632. 
  18. ↑ Lee, S K; Anzick S L, Choi J E, Bubendorf L, Guan X Y, Jung Y K, Kallioniemi O P, Kononen J, Trent J M, Azorsa D, Jhun B H, Cheong J H, Lee Y C, Meltzer P S, Lee J W (Nov. de 1999). «A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo». J. Biol. Chem. (UNITED STATES) 274 (48): 34283-93. ISSN 0021-9258. PMID 10567404. 
  19. ↑ Lee, S K; Jung S Y, Kim Y S, Na S Y, Lee Y C, Lee J W (Feb. de 2001). «Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2». Mol. Endocrinol. (United States) 15 (2): 241-54. ISSN 0888-8809. PMID 11158331. 
  20. ↑ Kong, Hee Jeong; Park Min Jung, Hong SunHwa, Yu Hyun Jung, Lee Young Chul, Choi Young Hyun, Cheong JaeHun (Nov. de 2003). «Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2». Hepatology (United States) 38 (5): 1258-66. ISSN 0270-9139. PMID 14578865. doi:10.1053/jhep.2003.50451. 
  21. ↑ Ko, Lan; Cardona Guemalli R, Iwasaki Toshiharu, Bramlett Kelli S, Burris Thomas P, Chin William W (Jan. de 2002). «Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs». Mol. Endocrinol. (United States) 16 (1): 128-40. ISSN 0888-8809. PMID 11773444. 
  22. ↑ Monden, T; Wondisford F E, Hollenberg A N (Nov. de 1997). «Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein». J. Biol. Chem. (UNITED STATES) 272 (47): 29834-41. ISSN 0021-9258. PMID 9368056. 
  23. ↑ Jeyakumar, M; Tanen M R, Bagchi M K (Jun. de 1997). «Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor». Mol. Endocrinol. (UNITED STATES) 11 (6): 755-67. ISSN 0888-8809. PMID 9171239. 
  24. ↑ Benkoussa, Madjid; Brand Céline, Delmotte Marie-Hélène, Formstecher Pierre, Lefebvre Philippe (Jul. de 2002). «Retinoic acid receptors inhibit AP1 activation by regulating extracellular signal-regulated kinase and CBP recruitment to an AP1-responsive promoter». Mol. Cell. Biol. (United States) 22 (13): 4522-34. ISSN 0270-7306. PMID 12052862. 
  25. ↑ Bugge, T H; Pohl J, Lonnoy O, Stunnenberg H G (Apr. de 1992). «RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors». EMBO J. (ENGLAND) 11 (4): 1409-18. ISSN 0261-4189. PMID 1314167. 
  26. ↑ Lin, Bingzhen; Kolluri Siva Kumar, Lin Feng, Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun (Feb. de 2004). «Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3». Cell (United States) 116 (4): 527-40. ISSN 0092-8674. PMID 14980220. 
  27. ↑ Zeng, Musheng; Kumar Ajay, Meng Gaoyuan, Gao Qingshen, Dimri Goberdhan, Wazer David, Band Hamid, Band Vimla (Nov. de 2002). «Human papilloma virus 16 E6 oncoprotein inhibits retinoic X receptor-mediated transactivation by targeting human ADA3 coactivator». J. Biol. Chem. (United States) 277 (47): 45611-8. ISSN 0021-9258. PMID 12235159. doi:10.1074/jbc.M208447200. 
  28. ↑ Na, S Y; Choi H S, Kim J W, Na D S, Lee J W (Nov. de 1998). «Bcl3, an IkappaB protein, as a novel transcription coactivator of the retinoid X receptor». J. Biol. Chem. (UNITED STATES) 273 (47): 30933-8. ISSN 0021-9258. PMID 9812988. 
  29. ↑ Tontonoz, P; Graves R A, Budavari A I, Erdjument-Bromage H, Lui M, Hu E, Tempst P, Spiegelman B M (Dec. de 1994). «Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha». Nucleic Acids Res. (ENGLAND) 22 (25): 5628-34. ISSN 0305-1048. PMID 7838715. 
  30. ↑ Berger, J; Patel H V, Woods J, Hayes N S, Parent S A, Clemas J, Leibowitz M D, Elbrecht A, Rachubinski R A, Capone J P, Moller D E (Apr. de 2000). «A PPARgamma mutant serves as a dominant negative inhibitor of PPAR signaling and is localized in the nucleus». Mol. Cell. Endocrinol. (IRELAND) 162 (1-2): 57-67. ISSN 0303-7207. PMID 10854698. 
  31. ↑ Gampe, R T; Montana V G, Lambert M H, Miller A B, Bledsoe R K, Milburn M V, Kliewer S A, Willson T M, Xu H E (Mar. de 2000). «Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors». Mol. Cell (UNITED STATES) 5 (3): 545-55. ISSN 1097-2765. PMID 10882139. 
  32. ↑ Takano, Yukihiko; Adachi Seiji, Okuno Masataka, Muto Yoshinori, Yoshioka Takashi, Matsushima-Nishiwaki Rie, Tsurumi Hisashi, Ito Kenichi, Friedman Scott L, Moriwaki Hisataka, Kojima Soichi, Okano Yukio (Apr. de 2004). «The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity». J. Biol. Chem. (United States) 279 (18): 18926-34. ISSN 0021-9258. PMID 14981089. doi:10.1074/jbc.M309148200. 
  33. ↑ Delerive, Philippe; Wu Yifei, Burris Thomas P, Chin William W, Suen Chen S (Feb. de 2002). «PGC-1 functions as a transcriptional coactivator for the retinoid X receptors». J. Biol. Chem. (United States) 277 (6): 3913-7. ISSN 0021-9258. PMID 11714715. doi:10.1074/jbc.M109409200. 
  34. ↑ Monden, T; Kishi M, Hosoya T, Satoh T, Wondisford F E, Hollenberg A N, Yamada M, Mori M (Oct. de 1999). «p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) on peroxisome proliferator-activated receptor-gamma/RXR heterodimers». Mol. Endocrinol. (UNITED STATES) 13 (10): 1695-703. ISSN 0888-8809. PMID 10517671. 
  35. ↑ a b Seol, W; Choi H S, Moore D D (Jan. de 1995). «Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors». Mol. Endocrinol. (UNITED STATES) 9 (1): 72-85. ISSN 0888-8809. PMID 7760852. 
  36. ↑ Froeschlé, A; Alric S, Kitzmann M, Carnac G, Auradé F, Rochette-Egly C, Bonnieu A (Jul. de 1998). «Retinoic acid receptors and muscle b-HLH proteins: partners in retinoid-induced myogenesis». Oncogene (ENGLAND) 16 (26): 3369-78. ISSN 0950-9232. PMID 9692544. doi:10.1038/sj.onc.1201894. 
  37. ↑ Baudino, T A; Kraichely D M, Jefcoat S C, Winchester S K, Partridge N C, MacDonald P N (Jun. de 1998). «Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription». J. Biol. Chem. (UNITED STATES) 273 (26): 16434-41. ISSN 0021-9258. PMID 9632709. 
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