CREBBP

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Proteína de unión a CREB

Estructura tridimensional de la proteína CREBBP.
Estructuras disponibles
PDB Búsqueda en Ortholog: PDBeRCSB
Identificadores
Símbolos CREBBP (HUGO: 2348); CBP; RSTS; RTS
Identificadores externos OMIM600140 MGI1098280 HomoloGene68393 ChEMBL5747 GeneCardsGen CREBBP
Número EC 2.3.1.48
Locus Cr. 16 p13.3
Patrones de expresión RNA
PBB GE CREBBP 202160 at tn.png
PBB GE CREBBP 211808 s at tn.png
Mayor información
Ortología
Especies Humano Ratón
Entrez 1387 12914
Ensembl Véase HS Véase MM
UniProt Q92793 F8VPR5
RefSeq (mRNA) NM_001079846 NM_001025432
RefSeq (proteína) NCBI NP_001073315 NP_001020603
Ubicación (UCSC) Chr 16:
3.78 – 3.93 Mb
Chr 16:
4.08 – 4.21 Mb
PubMed (búsqueda) [1] [2]

La proteína de unión a CREB, también conocido como CREBBP o CBP es una proteína codificada en humanos por el gen CREBBP.[1] [2]

Función[editar]

Este gen es expresado ubicuamente y está implicado en la co-activación transcripcional de diversos factores de transcripción. El primero fue aislado como una proteína nuclear que se une a proteínas de unión a elementos de respuesta a AMPc (CREB). Este gen es conocido por jugar un papel crítico en el desarrollo embrionario, el control de la proliferación celular y la homeostasis por medio de la reorganización de la cromatina para el reconocimiento de los factores de transcripción. Esta proteína posee una actividad histona acetiltransferasa intrínseca y actúa a su vez como andamio para estabilizar interacciones de proteínas adicionales con el complejo transcripcional. Esta proteína acetila tanto a histonas como a proteínas no histonas. Las CREBBP comparten regiones de una elevada similitud de secuencia con el bromodominio, las regiones ricas en cisteína-histidina y el dominio histona acetiltransferasa de la proteína EP300.[3]

Importancia clínica[editar]

Mutaciones en este gen son las causantes del síndrome de Rubinstein-Taybi (RTS).[4] Se han asociado diversas traslocaciones cromosómicas de este gen con la leucemia mieloide aguda.[3] [5]

Interacciones[editar]

La proteína CREBBP ha demostrado ser capaz de interaccionar con:

Véase también[editar]

Referencias[editar]

  1. Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH (October 1993). «Phosphorylated CREB binds specifically to the nuclear protein CBP». Nature 365 (6449):  pp. 855–9. doi:10.1038/365855a0. PMID 8413673. 
  2. Wydner KL, Bhattacharya S, Eckner R, Lawrence JB, Livingston DM (November 1995). «Localization of human CREB-binding protein gene (CREBBP) to 16p13.2-p13.3 by fluorescence in situ hybridization». Genomics 30 (2):  pp. 395–6. PMID 8586450. 
  3. a b «Entrez Gene: CREBBP (CREB-binding protein)».
  4. Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ (July 1995). «Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP». Nature 376 (6538):  pp. 348–51. doi:10.1038/376348a0. PMID 7630403. 
  5. Vizmanos JL, Larráyoz MJ, Lahortiga I, Floristán F, Alvarez C, Odero MD, Novo FJ, Calasanz MJ (April 2003). «t(10;16)(q22;p13) and MORF-CREBBP fusion is a recurrent event in acute myeloid leukemia». Genes Chromosomes Cancer 36 (4):  pp. 402–5. doi:10.1002/gcc.10174. PMID 12619164. 
  6. a b c Sano, Y; Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (Oct. 1998). «CBP alleviates the intramolecular inhibition of ATF-2 function». J. Biol. Chem. (UNITED STATES) 273 (44):  pp. 29098–105. doi:10.1074/jbc.273.44.29098. ISSN 0021-9258. PMID 9786917. 
  7. a b Kim, J; Jia L, Stallcup M R, Coetzee G A (Feb. 2005). «The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus». J. Mol. Endocrinol. (England) 34 (1):  pp. 107–18. doi:10.1677/jme.1.01701. ISSN 0952-5041. PMID 15691881. 
  8. Frønsdal, K; Engedal N, Slagsvold T, Saatcioglu F (Nov. 1998). «CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1». J. Biol. Chem. (UNITED STATES) 273 (48):  pp. 31853–9. doi:10.1074/jbc.273.48.31853. ISSN 0021-9258. PMID 9822653. 
  9. Ishitani, Ken; Yoshida Tasuku, Kitagawa Hirochika, Ohta Hiroaki, Nozawa Shiro, Kato Shigeaki (Jul. 2003). «p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor». Biochem. Biophys. Res. Commun. (United States) 306 (3):  pp. 660–5. doi:10.1016/S0006-291X(03)01021-0. ISSN 0006-291X. PMID 12810069. 
  10. a b Aarnisalo, P; Palvimo J J, Jänne O A (Mar. 1998). «CREB-binding protein in androgen receptor-mediated signaling». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (5):  pp. 2122–7. doi:10.1073/pnas.95.5.2122. ISSN 0027-8424. PMID 9482849. 
  11. Pitkänen, J; Doucas V, Sternsdorf T, Nakajima T, Aratani S, Jensen K, Will H, Vähämurto P, Ollila J, Vihinen M, Scott H S, Antonarakis S E, Kudoh J, Shimizu N, Krohn K, Peterson P (Jun. 2000). «The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein». J. Biol. Chem. (UNITED STATES) 275 (22):  pp. 16802–9. doi:10.1074/jbc.M908944199. ISSN 0021-9258. PMID 10748110. 
  12. Iioka, Takashi; Furukawa Keizo, Yamaguchi Akira, Shindo Hiroyuki, Yamashita Shunichi, Tsukazaki Tomoo (Aug. 2003). «P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain». J. Bone Miner. Res. (United States) 18 (8):  pp. 1419–29. doi:10.1359/jbmr.2003.18.8.1419. ISSN 0884-0431. PMID 12929931. 
  13. a b c Fan, Saijun; Ma Yong Xian, Wang Chenguang, Yuan Ren-Qi, Meng Qinghui, Wang Ji-An, Erdos Michael, Goldberg Itzhak D, Webb Paul, Kushner Peter J, Pestell Richard G, Rosen Eliot M (Jan. 2002). «p300 Modulates the BRCA1 inhibition of estrogen receptor activity». Cancer Res. (United States) 62 (1):  pp. 141–51. ISSN 0008-5472. PMID 11782371. 
  14. Pao, G M; Janknecht R, Ruffner H, Hunter T, Verma I M (Feb. 2000). «CBP/p300 interact with and function as transcriptional coactivators of BRCA1». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (3):  pp. 1020–5. doi:10.1073/pnas.97.3.1020. ISSN 0027-8424. PMID 10655477. 
  15. Chai, Y L; Cui J, Shao N, Shyam E, Reddy P, Rao V N (Jan. 1999). «The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter». Oncogene (ENGLAND) 18 (1):  pp. 263–8. doi:10.1038/sj.onc.1202323. ISSN 0950-9232. PMID 9926942. 
  16. Benezra, Miriam; Chevallier Nathalie, Morrison Debra J, MacLachlan Timothy K, El-Deiry Wafik S, Licht Jonathan D (Jul. 2003). «BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit». J. Biol. Chem. (United States) 278 (29):  pp. 26333–41. doi:10.1074/jbc.M303076200. ISSN 0021-9258. PMID 12700228. 
  17. a b Neish, A S; Anderson S F, Schlegel B P, Wei W, Parvin J D (Feb. 1998). «Factors associated with the mammalian RNA polymerase II holoenzyme». Nucleic Acids Res. (ENGLAND) 26 (3):  pp. 847–53. doi:10.1093/nar/26.3.847. ISSN 0305-1048. PMID 9443979. 
  18. Kawabuchi, M; Satomi Y, Takao T, Shimonishi Y, Nada S, Nagai K, Tarakhovsky A, Okada M (Apr. 2000). «Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases». Nature (ENGLAND) 404 (6781):  pp. 999–1003. doi:10.1038/35010121. ISSN 0028-0836. PMID 10801129. 
  19. a b Yamaguchi, Y; Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (Aug. 1998). «Casein kinase II interacts with the bZIP domains of several transcription factors». Nucleic Acids Res. (ENGLAND) 26 (16):  pp. 3854–61. doi:10.1093/nar/26.16.3854. ISSN 0305-1048. PMID 9685505. 
  20. Kovacs KA, Steinmann M; Magistretti PJ, Halfon O, Cardinaux JR (Sept. 2003). «CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation». J Biol. Chem. (UNITED STATES) 278 (38):  pp. 36959–65. doi:10.1074/jbc.M303147200. ISSN 0021-9258. PMID 12857754. 
  21. Lorentz, O; Suh E R, Taylor J K, Boudreau F, Traber P G (Mar. 1999). «CREB-binding [corrected] protein interacts with the homeodomain protein Cdx2 and enhances transcriptional activity». J. Biol. Chem. (UNITED STATES) 274 (11):  pp. 7196–9. doi:10.1074/jbc.274.11.7196. ISSN 0021-9258. PMID 10066780. 
  22. Shi, Yuling; Venkataraman Sujatha L, Dodson Gerald E, Mabb Angela M, LeBlanc Scott, Tibbetts Randal S (Apr. 2004). «Direct regulation of CREB transcriptional activity by ATM in response to genotoxic stress». Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (16):  pp. 5898–903. doi:10.1073/pnas.0307718101. ISSN 0027-8424. PMID 15073328. 
  23. Shimomura, A; Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (Jul. 1996). «Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein». J. Biol. Chem. (UNITED STATES) 271 (30):  pp. 17957–60. doi:10.1074/jbc.271.30.17957. ISSN 0021-9258. PMID 8663317. 
  24. Radhakrishnan, I; Pérez-Alvarado G C, Parker D, Dyson H J, Montminy M R, Wright P E (Dec. 1997). «Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions». Cell (UNITED STATES) 91 (6):  pp. 741–52. doi:10.1016/S0092-8674(00)80463-8. ISSN 0092-8674. PMID 9413984. 
  25. a b Zor, Tsaffrir; Mayr Bernhard M, Dyson H Jane, Montminy Marc R, Wright Peter E (Nov. 2002). «Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators». J. Biol. Chem. (United States) 277 (44):  pp. 42241–8. doi:10.1074/jbc.M207361200. ISSN 0021-9258. PMID 12196545. 
  26. a b Giebler, H A; Lemasson I, Nyborg J K (Jul. 2000). «p53 recruitment of CREB binding protein mediated through phosphorylated CREB: a novel pathway of tumor suppressor regulation». Mol. Cell. Biol. (UNITED STATES) 20 (13):  pp. 4849–58. doi:10.1128/MCB.20.13.4849-4858.2000. ISSN 0270-7306. PMID 10848610. 
  27. a b Zhang, Q; Vo N, Goodman R H (Jul. 2000). «Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB». Mol. Cell. Biol. (UNITED STATES) 20 (14):  pp. 4970–8. doi:10.1128/MCB.20.14.4970-4978.2000. ISSN 0270-7306. PMID 10866654. 
  28. a b Ernst, P; Wang J, Huang M, Goodman R H, Korsmeyer S J (Apr. 2001). «MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein». Mol. Cell. Biol. (United States) 21 (7):  pp. 2249–58. doi:10.1128/MCB.21.7.2249-2258.2001. ISSN 0270-7306. PMID 11259575. 
  29. Ledo, Fran; Kremer Leonor, Mellström Britt, Naranjo Jose R (Sep. 2002). «Ca2+-dependent block of CREB-CBP transcription by repressor DREAM». EMBO J. (England) 21 (17):  pp. 4583–92. doi:10.1093/emboj/cdf440. ISSN 0261-4189. PMID 12198160. 
  30. Li, S; Aufiero B, Schiltz R L, Walsh M J (Jun. 2000). «Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (13):  pp. 7166–71. doi:10.1073/pnas.130028697. ISSN 0027-8424. PMID 10852958. 
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  33. a b Sheppard, H M; Harries J C, Hussain S, Bevan C, Heery D M (Jan. 2001). «Analysis of the steroid receptor coactivator 1 (SRC1)-CREB binding protein interaction interface and its importance for the function of SRC1». Mol. Cell. Biol. (UNITED STATES) 21 (1):  pp. 39–50. doi:10.1128/MCB.21.1.39-50.2001. ISSN 0270-7306. PMID 11113179. 
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