Zufallsbild: Dirk Hoenes / Pixabay

CREB-Binding-Protein

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CREB-Binding-Protein

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Vorhandene Strukturdaten: s. UniProt
Eigenschaften des menschlichen Proteins
Masse/Länge Primärstruktur 2442 Aminosäuren
Bezeichner
Gen-Name CREBBP
Externe IDs OMIM: 600140 UniProt: Q92793
Enzymklassifikation
EC, Kategorie 2.3.1.48  Acetyltransferase
Reaktionsart Übertragung einer Acetylgruppe
Substrat Histon + Acetyl-CoA
Produkte Acetylhiston + CoA
Vorkommen
Homologie-Familie CREBBP
Übergeordnetes Taxon Euteleostomi

Das CREB-Binding Protein (CREB-Bindeprotein), kurz CBP, ist ein Coaktivator der Transkription.

CBP stellt eine Verbindung zwischen dem Transkriptionsfaktor CREB und dem Transkriptionsstartpunkt her, indem es als Histon-Acetyltransferase (HAT, EC 2.3.1.48) die Chromatin-Struktur verändert, die dadurch aufgelockert wird. CBP zeigt Homologien zum ebenfalls als HAT wirkendem Protein p300. CBP und p300 acetylieren bevorzugt die Histone H3 und H4.

CBP ist ein Coaktivator allgemeiner Natur und wechselwirkt z. B. auch mit Transkriptionsfaktoren.

Klinische Bedeutung

Mutationen in diesem Gen sind für das Rubinstein-Taybi-Syndrom (RTS) verantwortlich.[1]

Interaktionen

Das CREB-Bindeprotein weist Interaktion mit folgenden Proteinen auf:

Siehe auch

Einzelnachweise

  1. ↑ Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ: Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. In: Nature. 376, Nr. 6538, Juli 1995, S. 348–51. Bibcode: 1995Natur.376..348P. doi:10.1038/376348a0. PMID 7630403.
  2. ↑ 2,0 2,1 2,2 Y Sano, Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S: CBP alleviates the intramolecular inhibition of ATF-2 function. In: J. Biol. Chem.. 273, Nr. 44, UNITED STATES, Oktober 1998, S. 29098–105. doi:10.1074/jbc.273.44.29098. PMID 9786917.
  3. ↑ 3,0 3,1 J Kim, Jia L, Stallcup M R, Coetzee G A: The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus. In: J. Mol. Endocrinol.. 34, Nr. 1, England, Februar 2005, S. 107–18. doi:10.1677/jme.1.01701. PMID 15691881.
  4. ↑ K Frønsdal, Engedal N, Slagsvold T, Saatcioglu F: CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1. In: J. Biol. Chem.. 273, Nr. 48, UNITED STATES, November 1998, S. 31853–9. doi:10.1074/jbc.273.48.31853. PMID 9822653.
  5. ↑ Ken Ishitani, Yoshida Tasuku, Kitagawa Hirochika, Ohta Hiroaki, Nozawa Shiro, Kato Shigeaki: p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor. In: Biochem. Biophys. Res. Commun.. 306, Nr. 3, United States, Juli 2003, S. 660–5. doi:10.1016/S0006-291X(03)01021-0. PMID 12810069.
  6. ↑ 6,0 6,1 P Aarnisalo, Palvimo J J, Jänne O A: CREB-binding protein in androgen receptor-mediated signaling. In: Proc. Natl. Acad. Sci. U.S.A.. 95, Nr. 5, UNITED STATES, März 1998, S. 2122–7. Bibcode: 1998PNAS...95.2122A. doi:10.1073/pnas.95.5.2122. PMID 9482849. Volltext bei PMC: 19270.
  7. ↑ J Pitkänen, 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: The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein. In: J. Biol. Chem.. 275, Nr. 22, UNITED STATES, Juni 2000, S. 16802–9. doi:10.1074/jbc.M908944199. PMID 10748110.
  8. ↑ Takashi Iioka, Furukawa Keizo, Yamaguchi Akira, Shindo Hiroyuki, Yamashita Shunichi, Tsukazaki Tomoo: 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. In: J. Bone Miner. Res.. 18, Nr. 8, United States, August 2003, S. 1419–29. doi:10.1359/jbmr.2003.18.8.1419. PMID 12929931.
  9. ↑ 9,0 9,1 9,2 Saijun Fan, 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: p300 Modulates the BRCA1 inhibition of estrogen receptor activity. In: Cancer Res.. 62, Nr. 1, United States, Januar 2002, S. 141–51. PMID 11782371.
  10. ↑ G M Pao, Janknecht R, Ruffner H, Hunter T, Verma I M: CBP/p300 interact with and function as transcriptional coactivators of BRCA1. In: Proc. Natl. Acad. Sci. U.S.A.. 97, Nr. 3, UNITED STATES, Februar 2000, S. 1020–5. Bibcode: 2000PNAS...97.1020P. doi:10.1073/pnas.97.3.1020. PMID 10655477. Volltext bei PMC: 15508.
  11. ↑ Y L Chai, Cui J, Shao N, Shyam E, Reddy P, Rao V N: The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter. In: Oncogene. 18, Nr. 1, ENGLAND, Januar 1999, S. 263–8. doi:10.1038/sj.onc.1202323. PMID 9926942.
  12. ↑ Miriam Benezra, Chevallier Nathalie, Morrison Debra J, MacLachlan Timothy K, El-Deiry Wafik S, Licht Jonathan D: BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit. In: J. Biol. Chem.. 278, Nr. 29, United States, Juli 2003, S. 26333–41. doi:10.1074/jbc.M303076200. PMID 12700228.
  13. ↑ 13,0 13,1 A S Neish, Anderson S F, Schlegel B P, Wei W, Parvin J D: Factors associated with the mammalian RNA polymerase II holoenzyme. In: Nucleic Acids Res.. 26, Nr. 3, ENGLAND, Februar 1998, S. 847–53. doi:10.1093/nar/26.3.847. PMID 9443979. Volltext bei PMC: 147327.
  14. ↑ M Kawabuchi, Satomi Y, Takao T, Shimonishi Y, Nada S, Nagai K, Tarakhovsky A, Okada M: Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. In: Nature. 404, Nr. 6781, ENGLAND, April 2000, S. 999–1003. doi:10.1038/35010121. PMID 10801129.
  15. ↑ 15,0 15,1 Y Yamaguchi, Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H: Casein kinase II interacts with the bZIP domains of several transcription factors. In: Nucleic Acids Res.. 26, Nr. 16, ENGLAND, August 1998, S. 3854–61. doi:10.1093/nar/26.16.3854. PMID 9685505. Volltext bei PMC: 147779.
  16. ↑ Steinmann M Kovacs KA, Magistretti PJ, Halfon O, Cardinaux JR: CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation. In: J Biol. Chem.. 278, Nr. 38, UNITED STATES, Sept. 2003, S. 36959–65. doi:10.1074/jbc.M303147200. PMID 12857754.
  17. ↑ O Lorentz, Suh E R, Taylor J K, Boudreau F, Traber P G: CREB-binding [corrected] protein interacts with the homeodomain protein Cdx2 and enhances transcriptional activity. In: J. Biol. Chem.. 274, Nr. 11, UNITED STATES, März 1999, S. 7196–9. doi:10.1074/jbc.274.11.7196. PMID 10066780.
  18. ↑ Yuling Shi, Venkataraman Sujatha L, Dodson Gerald E, Mabb Angela M, LeBlanc Scott, Tibbetts Randal S: Direct regulation of CREB transcriptional activity by ATM in response to genotoxic stress. In: Proc. Natl. Acad. Sci. U.S.A.. 101, Nr. 16, United States, April 2004, S. 5898–903. Bibcode: 2004PNAS..101.5898S. doi:10.1073/pnas.0307718101. PMID 15073328. Volltext bei PMC: 395895.
  19. ↑ A Shimomura, Ogawa Y, Kitani T, Fujisawa H, Hagiwara M: Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein. In: J. Biol. Chem.. 271, Nr. 30, UNITED STATES, Juli 1996, S. 17957–60. doi:10.1074/jbc.271.30.17957. PMID 8663317.
  20. ↑ I Radhakrishnan, Pérez-Alvarado G C, Parker D, Dyson H J, Montminy M R, Wright P E: Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. In: Cell. 91, Nr. 6, UNITED STATES, Dezember 1997, S. 741–52. doi:10.1016/S0092-8674(00)80463-8. PMID 9413984.
  21. ↑ 21,0 21,1 Tsaffrir Zor, Mayr Bernhard M, Dyson H Jane, Montminy Marc R, Wright Peter E: 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. In: J. Biol. Chem.. 277, Nr. 44, United States, November 2002, S. 42241–8. doi:10.1074/jbc.M207361200. PMID 12196545.
  22. ↑ 22,0 22,1 H A Giebler, Lemasson I, Nyborg J K: p53 recruitment of CREB binding protein mediated through phosphorylated CREB: a novel pathway of tumor suppressor regulation. In: Mol. Cell. Biol.. 20, Nr. 13, UNITED STATES, Juli 2000, S. 4849–58. doi:10.1128/MCB.20.13.4849-4858.2000. PMID 10848610. Volltext bei PMC: 85936.
  23. ↑ 23,0 23,1 Q Zhang, Vo N, Goodman R H: Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB. In: Mol. Cell. Biol.. 20, Nr. 14, UNITED STATES, Juli 2000, S. 4970–8. doi:10.1128/MCB.20.14.4970-4978.2000. PMID 10866654. Volltext bei PMC: 85947.
  24. ↑ 24,0 24,1 P Ernst, Wang J, Huang M, Goodman R H, Korsmeyer S J: MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein. In: Mol. Cell. Biol.. 21, Nr. 7, United States, April 2001, S. 2249–58. doi:10.1128/MCB.21.7.2249-2258.2001. PMID 11259575. Volltext bei PMC: 86859.
  25. ↑ Fran Ledo, Kremer Leonor, Mellström Britt, Naranjo Jose R: Ca2+-dependent block of CREB-CBP transcription by repressor DREAM. In: EMBO J.. 21, Nr. 17, England, September 2002, S. 4583–92. doi:10.1093/emboj/cdf440. PMID 12198160. Volltext bei PMC: 126180.
  26. ↑ S Li, Aufiero B, Schiltz R L, Walsh M J: Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP. In: Proc. Natl. Acad. Sci. U.S.A.. 97, Nr. 13, UNITED STATES, Juni 2000, S. 7166–71. Bibcode: 2000PNAS...97.7166L. doi:10.1073/pnas.130028697. PMID 10852958. Volltext bei PMC: 16517.
  27. ↑ 27,0 27,1 27,2 27,3 H Cho, Orphanides G, Sun X, Yang X J, Ogryzko V, Lees E, Nakatani Y, Reinberg D: A human RNA polymerase II complex containing factors that modify chromatin structure. In: Mol. Cell. Biol.. 18, Nr. 9, UNITED STATES, September 1998, S. 5355–63. PMID 9710619. Volltext bei PMC: 109120.
  28. ↑ Fang Zhao, McCarrick-Walmsley Ruth, Akerblad Peter, Sigvardsson Mikael, Kadesch Tom: Inhibition of p300/CBP by early B-cell factor. In: Mol. Cell. Biol.. 23, Nr. 11, United States, Juni 2003, S. 3837–46. doi:10.1128/MCB.23.11.3837-3846.2003. PMID 12748286. Volltext bei PMC: 155219.
  29. ↑ 29,0 29,1 H M Sheppard, Harries J C, Hussain S, Bevan C, Heery D M: Analysis of the steroid receptor coactivator 1 (SRC1)-CREB binding protein interaction interface and its importance for the function of SRC1. In: Mol. Cell. Biol.. 21, Nr. 1, UNITED STATES, Januar 2001, S. 39–50. doi:10.1128/MCB.21.1.39-50.2001. PMID 11113179. Volltext bei PMC: 86566.
  30. ↑ S Chakraborty, Senyuk V, Sitailo S, Chi Y, Nucifora G: 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. In: J. Biol. Chem.. 276, Nr. 48, United States, November 2001, S. 44936–43. doi:10.1074/jbc.M106733200. PMID 11568182.
  31. ↑ N Nasrin, Ogg S, Cahill C M, Biggs W, Nui S, Dore J, Calvo D, Shi Y, Ruvkun G, Alexander-Bridges M C: DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in HepG2 cells. In: Proc. Natl. Acad. Sci. U.S.A.. 97, Nr. 19, UNITED STATES, September 2000, S. 10412–7. Bibcode: 2000PNAS...9710412N. doi:10.1073/pnas.190326997. PMID 10973497. Volltext bei PMC: 27038.
  32. ↑ P Dai, Akimaru H, Tanaka Y, Maekawa T, Nakafuku M, Ishii S: Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3. In: J. Biol. Chem.. 274, Nr. 12, UNITED STATES, März 1999, S. 8143–52. doi:10.1074/jbc.274.12.8143. PMID 10075717.
  33. ↑ T Almlöf, Wallberg A E, Gustafsson J A, Wright A P: Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor tau 1-core activation domain and target factors. In: Biochemistry. 37, Nr. 26, UNITED STATES, Juni 1998, S. 9586–94. doi:10.1021/bi973029x. PMID 9649342.
  34. ↑ E Yoshida, Aratani S, Itou H, Miyagishi M, Takiguchi M, Osumu T, Murakami K, Fukamizu A: Functional association between CBP and HNF4 in trans-activation. In: Biochem. Biophys. Res. Commun.. 241, Nr. 3, UNITED STATES, Dezember 1997, S. 664–9. doi:10.1006/bbrc.1997.7871. PMID 9434765.
  35. ↑ H Dell, Hadzopoulou-Cladaras M: CREB-binding protein is a transcriptional coactivator for hepatocyte nuclear factor-4 and enhances apolipoprotein gene expression. In: J. Biol. Chem.. 274, Nr. 13, UNITED STATES, März 1999, S. 9013–21. doi:10.1074/jbc.274.13.9013. PMID 10085149.
  36. ↑ M Ema, Hirota K, Mimura J, Abe H, Yodoi J, Sogawa K, Poellinger L, Fujii-Kuriyama Y: Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. In: EMBO J.. 18, Nr. 7, ENGLAND, April 1999, S. 1905–14. doi:10.1093/emboj/18.7.1905. PMID 10202154. Volltext bei PMC: 1171276.
  37. ↑ S Bhattacharya, Michels C L, Leung M K, Arany Z P, Kung A L, Livingston D M: Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. In: Genes Dev.. 13, Nr. 1, UNITED STATES, Januar 1999, S. 64–75. doi:10.1101/gad.13.1.64. PMID 9887100. Volltext bei PMC: 316375.
  38. ↑ Young-Kwon Park, Ahn Dae-Ro, Oh Myoungsuk, Lee Taekyoung, Yang Eun Gyeong, Son Miwon, Park Hyunsung: Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive hypoxia-inducible factor-1alpha by inhibiting von Hippel-Lindau recruitment and asparagine hydroxylation. In: Mol. Pharmacol.. 74, Nr. 1, United States, Juli 2008, S. 236–45. doi:10.1124/mol.108.045278. PMID 18426857.
  39. ↑ Thomas G Hofmann, Möller Andreas, Sirma Hüaeyin, Zentgraf Hanswalter, Taya Yoichi, Dröge Wulf, Will Hans, Schmitz M Lienhard: Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. In: Nat. Cell Biol.. 4, Nr. 1, England, Januar 2002, S. 1–10. doi:10.1038/ncb715. PMID 11740489.
  40. ↑ E Soutoglou, Papafotiou G, Katrakili N, Talianidis I: Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins. In: J. Biol. Chem.. 275, Nr. 17, UNITED STATES, April 2000, S. 12515–20. doi:10.1074/jbc.275.17.12515. PMID 10777539.
  41. ↑ A Chariot, van Lint C, Chapelier M, Gielen J, Merville M P, Bours V: CBP and histone deacetylase inhibition enhance the transactivation potential of the HOXB7 homeodomain-containing protein. In: Oncogene. 18, Nr. 27, ENGLAND, Juli 1999, S. 4007–14. doi:10.1038/sj.onc.1202776. PMID 10435624.
  42. ↑ Diego Vieyra, 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: Human ING1 proteins differentially regulate histone acetylation. In: J. Biol. Chem.. 277, Nr. 33, United States, August 2002, S. 29832–9. doi:10.1074/jbc.M200197200. PMID 12015309.
  43. ↑ Wei Hong, Resnick Ross J, Rakowski Carrie, Shalloway David, Taylor Steven J, Blobel Gerd A: Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68. In: Mol. Cancer Res.. 1, Nr. 1, United States, November 2002, S. 48–55. PMID 12496368.
  44. ↑ Chao-Zhong Song, Keller Kimberly, Murata Ken, Asano Haruhiko, Stamatoyannopoulos George: Functional interaction between coactivators CBP/p300, PCAF, and transcription factor FKLF2. In: J. Biol. Chem.. 277, Nr. 9, United States, März 2002, S. 7029–36. doi:10.1074/jbc.M108826200. PMID 11748222. Volltext bei PMC: 2808425.
  45. ↑ D E Geiman, Ton-That H, Johnson J M, Yang V W: 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. In: Nucleic Acids Res.. 28, Nr. 5, ENGLAND, März 2000, S. 1106–13. doi:10.1093/nar/28.5.1106. PMID 10666450. Volltext bei PMC: 102607.
  46. ↑ N A Barlev, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman J L, Berger S L: Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex. In: Mol. Cell. Biol.. 18, Nr. 3, UNITED STATES, März 1998, S. 1349–58. PMID 9488450. Volltext bei PMC: 108848.
  47. ↑ Qin Chen, Dowhan Dennis H, Liang Dongcai, Moore David D, Overbeek Paul A: CREB-binding protein/p300 co-activation of crystallin gene expression. In: J. Biol. Chem.. 277, Nr. 27, United States, Juli 2002, S. 24081–9. doi:10.1074/jbc.M201821200. PMID 11943779.
  48. ↑ Natalie K Goto, Zor Tsaffrir, Martinez-Yamout Maria, Dyson H Jane, Wright Peter E: Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain. In: J. Biol. Chem.. 277, Nr. 45, United States, November 2002, S. 43168–74. doi:10.1074/jbc.M207660200. PMID 12205094.
  49. ↑ K L Pearson, Hunter T, Janknecht R: Activation of Smad1-mediated transcription by p300/CBP. In: Biochim. Biophys. Acta. 1489, Nr. 2-3, NETHERLANDS, Dezember 1999, S. 354–64. doi:10.1016/S0167-4781(99)00166-9. PMID 10673036.
  50. ↑ 50,0 50,1 Y Sun, Nadal-Vicens M, Misono S, Lin M Z, Zubiaga A, Hua X, Fan G, Greenberg M E: Neurogenin promotes neurogenesis and inhibits glial differentiation by independent mechanisms. In: Cell. 104, Nr. 3, United States, Februar 2001, S. 365–76. doi:10.1016/S0092-8674(01)00224-0. PMID 11239394.
  51. ↑ S Shetty, Takahashi T, Matsui H, Ayengar R, Raghow R: Transcriptional autorepression of Msx1 gene is mediated by interactions of Msx1 protein with a multi-protein transcriptional complex containing TATA-binding protein, Sp1 and cAMP-response-element-binding protein-binding protein (CBP/p300). In: Biochem. J.. 339, Nr. 3, ENGLAND, May. 1999, S. 751–8. doi:10.1042/0264-6021:3390751. PMID 10215616. Volltext bei PMC: 1220213.
  52. ↑ 52,0 52,1 M Bessa, Saville M K, Watson R J: Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator. In: Oncogene. 20, Nr. 26, England, Juni 2001, S. 3376–86. doi:10.1038/sj.onc.1204439. PMID 11423988.
  53. ↑ A Polesskaya, Naguibneva I, Duquet A, Bengal E, Robin P, Harel-Bellan A: Interaction between acetylated MyoD and the bromodomain of CBP and/or p300. In: Mol. Cell. Biol.. 21, Nr. 16, United States, August 2001, S. 5312–20. doi:10.1128/MCB.21.16.5312-5320.2001. PMID 11463815. Volltext bei PMC: 87255.
  54. ↑ V Sartorelli, Huang J, Hamamori Y, Kedes L: Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C. In: Mol. Cell. Biol.. 17, Nr. 2, UNITED STATES, Februar 1997, S. 1010–26. PMID 9001254. Volltext bei PMC: 231826.
  55. ↑ S K Lee, 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: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. In: J. Biol. Chem.. 274, Nr. 48, UNITED STATES, November 1999, S. 34283–93. doi:10.1074/jbc.274.48.34283. PMID 10567404.
  56. ↑ S K Lee, Jung S Y, Kim Y S, Na S Y, Lee Y C, Lee J W: Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2. In: Mol. Endocrinol.. 15, Nr. 2, United States, Februar 2001, S. 241–54. doi:10.1210/me.15.2.241. PMID 11158331.
  57. ↑ T Yang, Davis R J, Chow C W: Requirement of two NFATc4 transactivation domains for CBP potentiation. In: J. Biol. Chem.. 276, Nr. 43, United States, Oktober 2001, S. 39569–76. doi:10.1074/jbc.M102961200. PMID 11514544.
  58. ↑ H L Hung, Kim A Y, Hong W, Rakowski C, Blobel G A: Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation. In: J. Biol. Chem.. 276, Nr. 14, United States, April 2001, S. 10715–21. doi:10.1074/jbc.M007846200. PMID 11154691.
  59. ↑ Y Katoh, Itoh K, Yoshida E, Miyagishi M, Fukamizu A, Yamamoto M: Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription. In: Genes Cells. 6, Nr. 10, England, Oktober 2001, S. 857–68. doi:10.1046/j.1365-2443.2001.00469.x. PMID 11683914.
  60. ↑ 60,0 60,1 Ray-Chang Wu, Qin Jun, Hashimoto Yoshihiro, Wong Jiemin, Xu Jianming, Tsai Sophia Y, Tsai Ming-Jer, O'Malley Bert W: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase. In: Mol. Cell. Biol.. 22, Nr. 10, United States, May. 2002, S. 3549–61. doi:10.1128/MCB.22.10.3549-3561.2002. PMID 11971985. Volltext bei PMC: 133790.
  61. ↑ A Naltner, Wert S, Whitsett J A, Yan C: Temporal/spatial expression of nuclear receptor coactivators in the mouse lung. In: Am. J. Physiol. Lung Cell Mol. Physiol.. 279, Nr. 6, UNITED STATES, Dezember 2000, S. L1066–74. PMID 11076796.
  62. ↑ L H Kasper, Brindle P K, Schnabel C A, Pritchard C E, Cleary M L, van Deursen J M: CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity. In: Mol. Cell. Biol.. 19, Nr. 1, UNITED STATES, Januar 1999, S. 764–76. PMID 9858599. Volltext bei PMC: 83933.
  63. ↑ Akihiro Ito, Kawaguchi Yoshiharu, Lai Chun-Hsiang, Kovacs Jeffrey J, Higashimoto Yuichiro, Appella Ettore, Yao Tso-Pang: MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation. In: EMBO J.. 21, Nr. 22, England, November 2002, S. 6236–45. doi:10.1093/emboj/cdf616. PMID 12426395. Volltext bei PMC: 137207.
  64. ↑ Jill A Livengood, Scoggin Kirsten E S, Van Orden Karen, McBryant Steven J, Edayathumangalam Rajeswari S, Laybourn Paul J, Nyborg Jennifer K: p53 Transcriptional activity is mediated through the SRC1-interacting domain of CBP/p300. In: J. Biol. Chem.. 277, Nr. 11, United States, März 2002, S. 9054–61. doi:10.1074/jbc.M108870200. PMID 11782467.
  65. ↑ 65,0 65,1 65,2 Marc Tini, Benecke Arndt, Um Soo-Joong, Torchia Joseph, Evans Ronald M, Chambon Pierre: Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. In: Mol. Cell. 9, Nr. 2, United States, Februar 2002, S. 265–77. doi:10.1016/S1097-2765(02)00453-7. PMID 11864601.
  66. ↑ P Puigserver, Adelmant G, Wu Z, Fan M, Xu J, O'Malley B, Spiegelman B M: Activation of PPARgamma coactivator-1 through transcription factor docking. In: Science. 286, Nr. 5443, UNITED STATES, November 1999, S. 1368–71. doi:10.1126/science.286.5443.1368. PMID 10558993.
  67. ↑ 67,0 67,1 Kazuhito Matsuzaki, Minami Takeshi, Tojo Masahide, Honda Yoshiomi, Saitoh Noriko, Nagahiro Shinji, Saya Hideyuki, Nakao Mitsuyoshi: PML-nuclear bodies are involved in cellular serum response. In: Genes Cells. 8, Nr. 3, England, März 2003, S. 275–86. doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724.
  68. ↑ V Doucas, Tini M, Egan D A, Evans R M: Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. In: Proc. Natl. Acad. Sci. U.S.A.. 96, Nr. 6, UNITED STATES, März 1999, S. 2627–32. Bibcode: 1999PNAS...96.2627D. doi:10.1073/pnas.96.6.2627. PMID 10077561. Volltext bei PMC: 15819.
  69. ↑ S Zhong, Delva L, Rachez C, Cenciarelli C, Gandini D, Zhang H, Kalantry S, Freedman L P, Pandolfi P P: A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins. In: Nat. Genet.. 23, Nr. 3, UNITED STATES, November 1999, S. 287–95. doi:10.1038/15463. PMID 10610177.
  70. ↑ Zoe Karetsou, Kretsovali Adroniki, Murphy Carol, Tsolas Orestes, Papamarcaki Thomais: Prothymosin alpha interacts with the CREB-binding protein and potentiates transcription. In: EMBO Rep.. 3, Nr. 4, England, April 2002, S. 361–6. doi:10.1093/embo-reports/kvf071. PMID 11897665. Volltext bei PMC: 1084059.
  71. ↑ Hyun Duk Jang, Yoon Kwiyeom, Shin Young Joo, Kim Jaesang, Lee Soo Young: PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit. In: J. Biol. Chem.. 279, Nr. 23, United States, Juni 2004, S. 24873–80. doi:10.1074/jbc.M313018200. PMID 15140884.
  72. ↑ Haihong Zhong, May Michael J, Jimi Eijiro, Ghosh Sankar: The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1. In: Mol. Cell. 9, Nr. 3, United States, März 2002, S. 625–36. doi:10.1016/S1097-2765(02)00477-X. PMID 11931769.
  73. ↑ G C Parry, Mackman N: Role of cyclic AMP response element-binding protein in cyclic AMP inhibition of NF-kappaB-mediated transcription. In: J. Immunol.. 159, Nr. 11, UNITED STATES, Dezember 1997, S. 5450–6. PMID 9548485.
  74. ↑ M E Gerritsen, Williams A J, Neish A S, Moore S, Shi Y, Collins T: CREB-binding protein/p300 are transcriptional coactivators of p65. In: Proc. Natl. Acad. Sci. U.S.A.. 94, Nr. 7, UNITED STATES, April 1997, S. 2927–32. Bibcode: 1997PNAS...94.2927G. doi:10.1073/pnas.94.7.2927. PMID 9096323. Volltext bei PMC: 20299.
  75. ↑ K Merienne, Pannetier S, Harel-Bellan A, Sassone-Corsi P: Mitogen-regulated RSK2-CBP interaction controls their kinase and acetylase activities. In: Mol. Cell. Biol.. 21, Nr. 20, United States, Oktober 2001, S. 7089–96. doi:10.1128/MCB.21.20.7089-7096.2001. PMID 11564891. Volltext bei PMC: 99884.
  76. ↑ Takuji Hirose, Fujii Ryouji, Nakamura Hiroshi, Aratani Satoko, Fujita Hidetoshi, Nakazawa Minako, Nakamura Kohzo, Nishioka Kusuki, Nakajima Toshihiro: Regulation of CREB-mediated transcription by association of CDK4 binding protein p34SEI-1 with CBP. In: Int. J. Mol. Med.. 11, Nr. 6, Greece, Juni 2003, S. 705–12. PMID 12736710.
  77. ↑ J DiRenzo, Shang Y, Phelan M, Sif S, Myers M, Kingston R, Brown M: BRG-1 is recruited to estrogen-responsive promoters and cooperates with factors involved in histone acetylation. In: Mol. Cell. Biol.. 20, Nr. 20, UNITED STATES, Oktober 2000, S. 7541–9. doi:10.1128/MCB.20.20.7541-7549.2000. PMID 11003650. Volltext bei PMC: 86306.
  78. ↑ 78,0 78,1 J D Oliner, Andresen J M, Hansen S K, Zhou S, Tjian R: SREBP transcriptional activity is mediated through an interaction with the CREB-binding protein. In: Genes Dev.. 10, Nr. 22, UNITED STATES, November 1996, S. 2903–11. doi:10.1101/gad.10.22.2903. PMID 8918891.
  79. ↑ Hiroyuki Aizawa, Hu Shu-Ching, Bobb Kathryn, Balakrishnan Karthik, Ince Gulayse, Gurevich Inga, Cowan Mitra, Ghosh Anirvan: Dendrite development regulated by CREST, a calcium-regulated transcriptional activator. In: Science. 303, Nr. 5655, United States, Januar 2004, S. 197–202. Bibcode: 2004Sci...303..197A. doi:10.1126/science.1089845. PMID 14716005.
  80. ↑ J J Zhang, Vinkemeier U, Gu W, Chakravarti D, Horvath C M, Darnell J E: Two contact regions between Stat1 and CBP/p300 in interferon gamma signaling. In: Proc. Natl. Acad. Sci. U.S.A.. 93, Nr. 26, UNITED STATES, Dezember 1996, S. 15092–6. Bibcode: 1996PNAS...9315092Z. doi:10.1073/pnas.93.26.15092. PMID 8986769. Volltext bei PMC: 26361.
  81. ↑ S Bhattacharya, Eckner R, Grossman S, Oldread E, Arany Z, D'Andrea A, Livingston D M: Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha. In: Nature. 383, Nr. 6598, ENGLAND, September 1996, S. 344–7. Bibcode: 1996Natur.383..344B. doi:10.1038/383344a0. PMID 8848048.
  82. ↑ C M Litterst, Pfitzner E: Transcriptional activation by STAT6 requires the direct interaction with NCoA-1. In: J. Biol. Chem.. 276, Nr. 49, United States, Dezember 2001, S. 45713–21. doi:10.1074/jbc.M108132200. PMID 11574547.
  83. ↑ C McDonald, Reich N C: Cooperation of the transcriptional coactivators CBP and p300 with Stat6. In: J. Interferon Cytokine Res.. 19, Nr. 7, UNITED STATES, Juli 1999, S. 711–22. doi:10.1089/107999099313550. PMID 10454341.
  84. ↑ Curtis Bradney, Hjelmeland Mark, Komatsu Yasuhiko, Yoshida Minoru, Yao Tso-Pang, Zhuang Yuan: Regulation of E2A activities by histone acetyltransferases in B lymphocyte development. In: J. Biol. Chem.. 278, Nr. 4, United States, Januar 2003, S. 2370–6. doi:10.1074/jbc.M211464200. PMID 12435739.
  85. ↑ Parimal Misra, Qi Chao, Yu Songtao, Shah Sejal H, Cao Wen-Qing, Rao M Sambasiva, Thimmapaya Bayar, Zhu Yijun, Reddy Janardan K: Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation. In: J. Biol. Chem.. 277, Nr. 22, United States, May. 2002, S. 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
  86. ↑ F Gizard, Lavallée B, DeWitte F, Hum D W: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. In: J. Biol. Chem.. 276, Nr. 36, United States, September 2001, S. 33881–92. doi:10.1074/jbc.M100113200. PMID 11349124.
  87. ↑ E S Silverman, Du J, Williams A J, Wadgaonkar R, Drazen J M, Collins T: cAMP-response-element-binding-protein-binding protein (CBP) and p300 are transcriptional co-activators of early growth response factor-1 (Egr-1). In: Biochem. J.. 336, Nr. 1, ENGLAND, November 1998, S. 183–9. PMID 9806899. Volltext bei PMC: 1219856.

Literatur

  • Rolf Knippers: Molekulare Genetik. 9. Auflage. Georg Thieme Verlag, 2006, ISBN 3-13-477009-1
  • Goldman PS, Tran VK, Goodman RH: The multifunctional role of the co-activator CBP in transcriptional regulation.. In: Recent Prog. Horm. Res.. 52, 1997, S. 103–19; discussion 119–20. PMID 9238849.
  • Marcello A, Zoppé M, Giacca M: Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.. In: IUBMB Life. 51, Nr. 3, 2002, S. 175–81. doi:10.1080/152165401753544241. PMID 11547919.
  • Matt T: Transcriptional control of the inflammatory response: a role for the CREB-binding protein (CBP).. In: Acta Med. Austriaca. 29, Nr. 3, 2002, S. 77–9. doi:10.1046/j.1563-2571.2002.02010.x. PMID 12168567.
  • Combes R, Balls M, Bansil L, et al.: An assessment of progress in the use of alternatives in toxicity testing since the publication of the report of the second FRAME Toxicity Committee (1991).. In: Alternatives to laboratory animals : ATLA. 30, Nr. 4, 2002, S. 365–406. PMID 12234245.
  • Minghetti L, Visentin S, Patrizio M, et al.: Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions.. In: Neurochem. Res.. 29, Nr. 5, 2004, S. 965–78. doi:10.1023/B:NERE.0000021241.90133.89. PMID 15139295.
  • Kino T, Pavlakis GN: Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.. In: DNA Cell Biol.. 23, Nr. 4, 2004, S. 193–205. doi:10.1089/104454904773819789. PMID 15142377.
  • Greene WC, Chen LF: Regulation of NF-kappaB action by reversible acetylation.. In: Novartis Found. Symp.. 259, 2004, S. 208–17; discussion 218–25. doi:10.1002/0470862637.ch15. PMID 15171256.
  • Liou LY, Herrmann CH, Rice AP: HIV-1 infection and regulation of Tat function in macrophages.. In: Int. J. Biochem. Cell Biol.. 36, Nr. 9, 2005, S. 1767–75. doi:10.1016/j.biocel.2004.02.018. PMID 15183343.
  • Pugliese A, Vidotto V, Beltramo T, et al.: A review of HIV-1 Tat protein biological effects.. In: Cell Biochem. Funct.. 23, Nr. 4, 2005, S. 223–7. doi:10.1002/cbf.1147. PMID 15473004.
  • Bannwarth S, Gatignol A: HIV-1 TAR RNA: the target of molecular interactions between the virus and its host.. In: Curr. HIV Res.. 3, Nr. 1, 2005, S. 61–71. doi:10.2174/1570162052772924. PMID 15638724.
  • Le Rouzic E, Benichou S: The Vpr protein from HIV-1: distinct roles along the viral life cycle.. In: Retrovirology. 2, 2006, S. 11. doi:10.1186/1742-4690-2-11. PMID 15725353. Volltext bei PMC: 554975.
  • Gibellini D, Vitone F, Schiavone P, Re MC: HIV-1 tat protein and cell proliferation and survival: a brief review.. In: New Microbiol.. 28, Nr. 2, 2005, S. 95–109. PMID 16035254.
  • Hetzer C, Dormeyer W, Schnölzer M, Ott M: Decoding Tat: the biology of HIV Tat posttranslational modifications.. In: Microbes Infect.. 7, Nr. 13, 2006, S. 1364–9. doi:10.1016/j.micinf.2005.06.003. PMID 16046164.
  • Peruzzi F: The multiple functions of HIV-1 Tat: proliferation versus apoptosis.. In: Front. Biosci.. 11, 2006, S. 708–17. doi:10.2741/1829. PMID 16146763.
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