CREB-bindingseiwit

Het CREB-bindingseiwit

Het CREB-bindingseiwit (CREB-Binding-Protein, afgekort CBP), is een co-activator bij de transcriptie.

Bij de mens wordt het CREB-bindingseiwit gecodeerd door het CREBBP-gen (ook wel CBP-gen genoemd).[1][2]

Het CREB-bindingseiwit heeft de volgende domeinen:

  • het nucleusreceptor interactie domein (RID),
  • het CREB en MYB interactie domein (KIX),
  • de cysteïne/histidine regio's (TAZ1/CH1 en TAZ2/CH3) en
  • het interferon reactiebindend domein (IBiD).

De CREB-bindingseiwit domeinen, KIX, TAZ1 en TAZ2 binden elk stevig aan de beide transactivatie domeinen 9aaTADs van de transcriptiefactor p53.[3][4]

Functie

Het CREBBP-gen is betrokken bij de transcriptionele coactivatie van veel verschillende transcriptiefactoren. Het werd voor het eerst geïsoleerd als een nucleuseiwit dat zich bindt aan het cAMP-reactie-elementbindend eiwit (CREB). Het gen speelt een kritische rol bij de embryonale ontwikkeling, controle van de groei en homeostase door te koppelen aan chromatine en het zo geschikt te maken voor de herkenning van de transcriptiefactor. Het door het gen gecodeerde eiwit heeft een eigen histon-acetyltransferase activiteit[5] en werkt ook ondersteunend voor het stabiliseren van bijkomende eiwitinteracties met het transcriptieomplex. Het eiwit acetyleert zowel histonen als non-histon eiwitten. Het eiwit heeft zeer sterk vergelijkbare regio's met het eiwit EP300 en hun bromodomein, cysteïne-histidine-rijke regio's en het histonacetyltransferasedomein.[6]

Klinisch belang

Mutaties in het CREBBP-gen is de oorzaak van het syndroom van Rubinstein-Taybi (RTS).[7] De chromosomale translocatie, waarbij het CREBBP-gen betrokken is, wordt in verband gebracht met acute myeloïde leukemie.[6][8]

Interacties

Het CREB-bindingseiwit vertoont interactie met de volgende eiwitten:

  • Activating transcription factor 2[9]
  • Androgen receptor[10][11][12][13]
  • Autoimmune regulator[14][15]
  • BRCA1[16][17][18][19][20]
  • BRCA2
  • C-jun[9]
  • C-src tyrosine kinase[21]
  • Casein kinase 2, alpha 1[22]
  • Ccaat-enhancer-binding proteins[23]
  • CDX2[24]
  • CREB1[9][10][25][26][27][28][29][30][31][32]
  • CSNK2A2[22]
  • CUTL1[33]
  • Cyclin-dependent kinase 8[34]
  • EBF1[35]
  • Estrogen receptor alpha[16][36]
  • EVI1[37]
  • FOXO1[38]
  • GLI3[39]
  • Glucocorticoid receptor[40]
  • Hepatocyte nuclear factor 4 alpha[41][42]
  • HIF1A[43][44][45]
  • HIPK2[46]
  • HNF1A[47]
  • HOXB7[48]
  • ING1[49]
  • KHDRBS1[50]
  • KLF13[51]
  • KLF4[52]
  • Ku70[53]
  • MAF[54]
  • MLL[31][55]
  • Mothers against decapentaplegic homolog 1[56][57]
  • MSX1[58]
  • MYB[28][59]
  • MYBL2[59]
  • MyoD[60][61]
  • NCOA6[62][63]
  • NEUROG1[57]
  • NFATC4[64]
  • NFE2[65]
  • NFE2L2[66]
  • Nuclear receptor coactivator 1[36][67]
  • Nuclear receptor coactivator 3[67][68]
  • NUP98[69]
  • P53[29][70][71]
  • PCAF[34][72]
  • POLR2A[34]
  • PPARGC1A[73]
  • Promyelocytic leukemia protein[74][75][76]
  • PTMA[77]
  • RBBP4[30]
  • RELA[13][78][79][80][81]
  • RPS6KA3[82]
  • SERTAD1[83]
  • Serum response factor[74]
  • SMARCB1[34]
  • SMARCA4[20][84]
  • SREBF1[85]
  • SREBF2[85]
  • SS18L1[86]
  • STAT1[87]
  • STAT2[88]
  • STAT6[89][90]
  • TCF3[91]
  • TGS1[92]
  • Thymine-DNA glycosylase[72]
  • Transcription Factor II B[16][72]
  • TRERF1[93]
  • Zif268.[94]
Bronnen, noten en/of referenties
  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): 855–9. PMID 8413673. DOI: 10.1038/365855a0.
  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): 395–6. PMID 8586450.
  3. ↑ Teufel DP, Freund SM, Bycroft M, Fersht AR (April 2007). Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. PNAS 104 (17): 7009–7014. PMID 17438265. PMC 1855428. DOI: 10.1073/pnas.0702010104. ; Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). Nine-amino-acid transactivation domain: establishment and prediction utilities. Genomics 89 (6): 756–68. PMID 17467953. DOI: 10.1016/j.ygeno.2007.02.003. ; Piskacek M (5 november 2009). 9aaTAD is a common transactivation domain recruits multiple general coactivators TAF9, MED15, CBP/p300 and GCN5. Nature Precedings Pre-publication. DOI: 10.1038/npre.2009.3488.2. ; Piskacek M (5 november 2009). 9aaTADs mimic DNA to interact with a pseudo-DNA Binding Domain KIX of Med15 (Molecular Chameleons). Nature Precedings Pre-publication. DOI: 10.1038/npre.2009.3939.1. ; Piskacek M (20 november 2009). 9aaTAD Prediction result (2006). Nature Precedings Pre-publication. DOI: 10.1038/npre.2009.3984.1.
  4. ↑ The prediction for 9aaTADs (for both acidic and hydrophilic transactivation domains) is available online from ExPASy https://web.archive.org/web/20100716130743/http://us.expasy.org/tools/ and EMBnet Spain https://archive.today/20130704002729/http://www.es.embnet.org/Services/EMBnetAT/htdoc/9aatad/
  5. ↑ Ogryzko VV et al. "The transcriptional coactivators p300 and CBP are histone acetyltransferases". Cell. 1996 87(5):953-9.[1]. Gearchiveerd op 19 maart 2020.
  6. ↑ a b Entrez Gene: CREBBP (CREB-binding protein).
  7. ↑ 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): 348–51. PMID 7630403. DOI: 10.1038/376348a0.
  8. ↑ 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): 402–5. PMID 12619164. DOI: 10.1002/gcc.10174.
  9. ↑ 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. 273 (44): 29098–105 (UNITED STATES)​. ISSN: 0021-9258. PMID 9786917. DOI: 10.1074/jbc.273.44.29098.
  10. ↑ 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. 34 (1): 107–18 (England)​. ISSN: 0952-5041. PMID 15691881. DOI: 10.1677/jme.1.01701.
  11. ↑ 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. 273 (48): 31853–9 (UNITED STATES)​. ISSN: 0021-9258. PMID 9822653. DOI: 10.1074/jbc.273.48.31853.
  12. ↑ 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. 306 (3): 660–5 (United States)​. ISSN: 0006-291X. PMID 12810069. DOI: 10.1016/S0006-291X(03)01021-0.
  13. ↑ 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. 95 (5): 2122–7 (UNITED STATES)​. ISSN: 0027-8424. PMID 9482849. PMC 19270. DOI: 10.1073/pnas.95.5.2122.
  14. ↑ 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. 275 (22): 16802–9 (UNITED STATES)​. ISSN: 0021-9258. PMID 10748110. DOI: 10.1074/jbc.M908944199.
  15. ↑ 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. 18 (8): 1419–29 (United States)​. ISSN: 0884-0431. PMID 12929931. DOI: 10.1359/jbmr.2003.18.8.1419.
  16. ↑ 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. 62 (1): 141–51 (United States)​. ISSN: 0008-5472. PMID 11782371.
  17. ↑ 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. 97 (3): 1020–5 (UNITED STATES)​. ISSN: 0027-8424. PMID 10655477. PMC 15508. DOI: 10.1073/pnas.97.3.1020.
  18. ↑ 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 18 (1): 263–8 (ENGLAND)​. ISSN: 0950-9232. PMID 9926942. DOI: 10.1038/sj.onc.1202323.
  19. ↑ 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. 278 (29): 26333–41 (United States)​. ISSN: 0021-9258. PMID 12700228. DOI: 10.1074/jbc.M303076200.
  20. ↑ 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. 26 (3): 847–53 (ENGLAND)​. ISSN: 0305-1048. PMID 9443979. PMC 147327. DOI: 10.1093/nar/26.3.847.
  21. ↑ 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 404 (6781): 999–1003 (ENGLAND)​. ISSN: 0028-0836. PMID 10801129. DOI: 10.1038/35010121.
  22. ↑ 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. 26 (16): 3854–61 (ENGLAND)​. ISSN: 0305-1048. PMID 9685505. PMC 147779. DOI: 10.1093/nar/26.16.3854.
  23. ↑ 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. 278 (38): 36959–65 (UNITED STATES)​. ISSN: 0021-9258. PMID 12857754. DOI: 10.1074/jbc.M303147200.
  24. ↑ 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. 274 (11): 7196–9 (UNITED STATES)​. ISSN: 0021-9258. PMID 10066780. DOI: 10.1074/jbc.274.11.7196.
  25. ↑ 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. 101 (16): 5898–903 (United States)​. ISSN: 0027-8424. PMID 15073328. PMC 395895. DOI: 10.1073/pnas.0307718101.
  26. ↑ 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. 271 (30): 17957–60 (UNITED STATES)​. ISSN: 0021-9258. PMID 8663317. DOI: 10.1074/jbc.271.30.17957.
  27. ↑ 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 91 (6): 741–52 (UNITED STATES)​. ISSN: 0092-8674. PMID 9413984. DOI: 10.1016/S0092-8674(00)80463-8.
  28. ↑ 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. 277 (44): 42241–8 (United States)​. ISSN: 0021-9258. PMID 12196545. DOI: 10.1074/jbc.M207361200.
  29. ↑ 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. 20 (13): 4849–58 (UNITED STATES)​. ISSN: 0270-7306. PMID 10848610. PMC 85936. DOI: 10.1128/MCB.20.13.4849-4858.2000.
  30. ↑ 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. 20 (14): 4970–8 (UNITED STATES)​. ISSN: 0270-7306. PMID 10866654. PMC 85947. DOI: 10.1128/MCB.20.14.4970-4978.2000.
  31. ↑ 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. 21 (7): 2249–58 (United States)​. ISSN: 0270-7306. PMID 11259575. PMC 86859. DOI: 10.1128/MCB.21.7.2249-2258.2001.
  32. ↑ Ledo, Fran, Kremer Leonor, Mellström Britt, Naranjo Jose R (Sep. 2002). Ca2+-dependent block of CREB-CBP transcription by repressor DREAM. EMBO J. 21 (17): 4583–92 (England)​. ISSN: 0261-4189. PMID 12198160. PMC 126180. DOI: 10.1093/emboj/cdf440.
  33. ↑ 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. 97 (13): 7166–71 (UNITED STATES)​. ISSN: 0027-8424. PMID 10852958. PMC 16517. DOI: 10.1073/pnas.130028697.
  34. ↑ a b c d Cho, H, Orphanides G, Sun X, Yang X J, Ogryzko V, Lees E, Nakatani Y, Reinberg D (Sep. 1998). A human RNA polymerase II complex containing factors that modify chromatin structure. Mol. Cell. Biol. 18 (9): 5355–63 (UNITED STATES)​. ISSN: 0270-7306. PMID 9710619. PMC 109120.
  35. ↑ Zhao, Fang, McCarrick-Walmsley Ruth, Akerblad Peter, Sigvardsson Mikael, Kadesch Tom (Jun. 2003). Inhibition of p300/CBP by early B-cell factor. Mol. Cell. Biol. 23 (11): 3837–46 (United States)​. ISSN: 0270-7306. PMID 12748286. PMC 155219. DOI: 10.1128/MCB.23.11.3837-3846.2003.
  36. ↑ 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. 21 (1): 39–50 (UNITED STATES)​. ISSN: 0270-7306. PMID 11113179. PMC 86566. DOI: 10.1128/MCB.21.1.39-50.2001.
  37. ↑ Chakraborty, S, Senyuk V, Sitailo S, Chi Y, Nucifora G (Nov. 2001). Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. J. Biol. Chem. 276 (48): 44936–43 (United States)​. ISSN: 0021-9258. PMID 11568182. DOI: 10.1074/jbc.M106733200.
  38. ↑ Nasrin, N, Ogg S, Cahill C M, Biggs W, Nui S, Dore J, Calvo D, Shi Y, Ruvkun G, Alexander-Bridges M C (Sep. 2000). DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in HepG2 cells. Proc. Natl. Acad. Sci. U.S.A. 97 (19): 10412–7 (UNITED STATES)​. ISSN: 0027-8424. PMID 10973497. PMC 27038. DOI: 10.1073/pnas.190326997.
  39. ↑ Dai, P, Akimaru H, Tanaka Y, Maekawa T, Nakafuku M, Ishii S (Mar. 1999). Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3. J. Biol. Chem. 274 (12): 8143–52 (UNITED STATES)​. ISSN: 0021-9258. PMID 10075717. DOI: 10.1074/jbc.274.12.8143.
  40. ↑ Almlöf, T, Wallberg A E, Gustafsson J A, Wright A P (Jun. 1998). Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors. Biochemistry 37 (26): 9586–94 (UNITED STATES)​. ISSN: 0006-2960. PMID 9649342. DOI: 10.1021/bi973029x.
  41. ↑ Yoshida, E, Aratani S, Itou H, Miyagishi M, Takiguchi M, Osumu T, Murakami K, Fukamizu A (Dec. 1997). Functional association between CBP and HNF4 in trans-activation. Biochem. Biophys. Res. Commun. 241 (3): 664–9 (UNITED STATES)​. ISSN: 0006-291X. PMID 9434765. DOI: 10.1006/bbrc.1997.7871.
  42. ↑ Dell, H, Hadzopoulou-Cladaras M (Mar. 1999). CREB-binding protein is a transcriptional coactivator for hepatocyte nuclear factor-4 and enhances apolipoprotein gene expression. J. Biol. Chem. 274 (13): 9013–21 (UNITED STATES)​. ISSN: 0021-9258. PMID 10085149. DOI: 10.1074/jbc.274.13.9013.
  43. ↑ Ema, M, Hirota K, Mimura J, Abe H, Yodoi J, Sogawa K, Poellinger L, Fujii-Kuriyama Y (Apr. 1999). Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J. 18 (7): 1905–14 (ENGLAND)​. ISSN: 0261-4189. PMID 10202154. PMC 1171276. DOI: 10.1093/emboj/18.7.1905.
  44. ↑ Bhattacharya, S, Michels C L, Leung M K, Arany Z P, Kung A L, Livingston D M (Jan. 1999). Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes Dev. 13 (1): 64–75 (UNITED STATES)​. ISSN: 0890-9369. PMID 9887100. PMC 316375. DOI: 10.1101/gad.13.1.64.
  45. ↑ Park, Young-Kwon, Ahn Dae-Ro, Oh Myoungsuk, Lee Taekyoung, Yang Eun Gyeong, Son Miwon, Park Hyunsung (Jul. 2008). Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive hypoxia-inducible factor-1alpha by inhibiting von Hippel-Lindau recruitment and asparagine hydroxylation. Mol. Pharmacol. 74 (1): 236–45 (United States)​. PMID 18426857. DOI: 10.1124/mol.108.045278.
  46. ↑ Hofmann, Thomas G, Möller Andreas, Sirma Hüaeyin, Zentgraf Hanswalter, Taya Yoichi, Dröge Wulf, Will Hans, Schmitz M Lienhard (Jan. 2002). Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. Nat. Cell Biol. 4 (1): 1–10 (England)​. ISSN: 1465-7392. PMID 11740489. DOI: 10.1038/ncb715.
  47. ↑ Soutoglou, E, Papafotiou G, Katrakili N, Talianidis I (Apr. 2000). Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins. J. Biol. Chem. 275 (17): 12515–20 (UNITED STATES)​. ISSN: 0021-9258. PMID 10777539. DOI: 10.1074/jbc.275.17.12515.
  48. ↑ Chariot, A, van Lint C, Chapelier M, Gielen J, Merville M P, Bours V (Jul. 1999). CBP and histone deacetylase inhibition enhance the transactivation potential of the HOXB7 homeodomain-containing protein. Oncogene 18 (27): 4007–14 (ENGLAND)​. ISSN: 0950-9232. PMID 10435624. DOI: 10.1038/sj.onc.1202776.
  49. ↑ Vieyra, Diego, Loewith Robbie, Scott Michelle, Bonnefin Paul, Boisvert Francois-Michel, Cheema Parneet, Pastyryeva Svitlana, Meijer Maria, Johnston Randal N, Bazett-Jones David P, McMahon Steven, Cole Michael D, Young Dallan, Riabowol Karl (Aug. 2002). Human ING1 proteins differentially regulate histone acetylation. J. Biol. Chem. 277 (33): 29832–9 (United States)​. ISSN: 0021-9258. PMID 12015309. DOI: 10.1074/jbc.M200197200.
  50. ↑ Hong, Wei, Resnick Ross J, Rakowski Carrie, Shalloway David, Taylor Steven J, Blobel Gerd A (Nov. 2002). Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68. Mol. Cancer Res. 1 (1): 48–55 (United States)​. ISSN: 1541-7786. PMID 12496368.
  51. ↑ Song, Chao-Zhong, Keller Kimberly, Murata Ken, Asano Haruhiko, Stamatoyannopoulos George (Mar. 2002). Functional interaction between coactivators CBP/p300, PCAF, and transcription factor FKLF2. J. Biol. Chem. 277 (9): 7029–36 (United States)​. ISSN: 0021-9258. PMID 11748222. PMC 2808425. DOI: 10.1074/jbc.M108826200.
  52. ↑ Geiman, D E, Ton-That H, Johnson J M, Yang V W (Mar. 2000). Transactivation and growth suppression by the gut-enriched Krüppel-like factor (Krüppel-like factor 4) are dependent on acidic amino acid residues and protein-protein interaction. Nucleic Acids Res. 28 (5): 1106–13 (ENGLAND)​. PMID 10666450. PMC 102607. DOI: 10.1093/nar/28.5.1106.
  53. ↑ Barlev, N A, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman J L, Berger S L (Mar. 1998). Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex. Mol. Cell. Biol. 18 (3): 1349–58 (UNITED STATES)​. ISSN: 0270-7306. PMID 9488450. PMC 108848.
  54. ↑ Chen, Qin, Dowhan Dennis H, Liang Dongcai, Moore David D, Overbeek Paul A (Jul. 2002). CREB-binding protein/p300 co-activation of crystallin gene expression. J. Biol. Chem. 277 (27): 24081–9 (United States)​. ISSN: 0021-9258. PMID 11943779. DOI: 10.1074/jbc.M201821200.
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