p300 Acts as a Transcriptional Coactivator for Mammalian Notch-1

REFERENCES

• Arias, J., A. S. Alberts, P. Brindle, F. X. Claret, T. Smeal, M. Karin, J. Feramisco, and M. Montminy. 1994. Activation of cAMP and mitogen responsive genes relies on a common nuclear factor. Nature 370:226–229.
   PubMed Web of Science ®Google Scholar
• Artavanis-Tsakonas, S., M. D. Rand, and R. J. Lake. 1999. Notch signaling: cell fate control and signal integration in development. Science 284:770–776.
   PubMed Web of Science ®Google Scholar
• Aster, J. C., E. S. Robertson, R. P. Hasserjian, J. R. Turner, E Kieff, and J. Sklar. 1997. Oncogenic forms of NOTCH1 lacking either the primary binding site for RBP-Jκ or nuclear localization sequences retain the ability to associate with RBP-Jκ and activate transcription. J. Biol. Chem. 272:11336–11343.
   PubMedGoogle Scholar
• Bailey, A. M., and J. W. Posakony. 1995. Suppressor of hairless directly activates transcription of enhancer of split complex genes in response to Notch receptor activity. Genes Dev. 9:2609–2622.
   PubMed Web of Science ®Google Scholar
• Beatus, P., J. Lundkvist, C. Oberg, and U. Lendahl. 1999. The notch 3 intracellular domain represses notch 1-mediated activation through Hairy/Enhancer of split (HES) promoters. Development 126:3925–3935.
   PubMedGoogle Scholar
• Capobianco, A. J., P. Zagouras, C. M. Blaumueller, S. Artavanis-Tsakonas, and J. M. Bishop. 1997. Neoplastic transformation by truncated alleles of human NOTCH1/TAN1 and NOTCH2. Mol. Cell. Biol. 17:6265–6273.
   PubMed Web of Science ®Google Scholar
• Chakravarti, D., V. J. LaMorte, M. C. Nelson, T. Nakajima, I. G. Schulman, H. Juguilon, M. Montminy, and R. M. Evans. 1996. Role of CBP/P300 in nuclear receptor signalling. Nature 383:99–103.
   PubMed Web of Science ®Google Scholar
• Chakravarti, D., V. Ogryzko, H. Y. Kao, A. Nash, H. Chen, Y. Nakatani, and R. M. Evans. 1999. A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity. Cell 96:393–403.
   PubMed Web of Science ®Google Scholar
• Dou, S., X. Zeng, P. Cortes, H. Erdjument-Bromage, P. Tempst, T. Honjo, and L. D. Vales. 1994. The recombination signal sequence-binding protein RBP-2N functions as a transcriptional repressor. Mol. Cell. Biol. 14:3310–3319.
   PubMedGoogle Scholar
• Dumont, E., K. P. Fuchs, G. Bommer, B. Christoph, E. Kremmer, and B. Kempkes. 2000. Neoplastic transformation by Notch is independent of transcriptional activation by RBP-J signalling. Oncogene 19:556–561.
   PubMedGoogle Scholar
• Egan, S. E., B. St. Pierre, and C. C. Leow. 1998. Notch receptors, partners and regulators: from conserved domains to powerful functions. Curr. Top. Microbiol. Immunol. 228:273–324.
   PubMed Web of Science ®Google Scholar
• Feng, X. H., Y. Zhang, R. Y. Wu, and R. Derynck. 1998. The tumor suppressor Smad4/DPC4 and transcriptional adaptor CBP/p300 are coactivators for smad3 in TGF-β-induced transcriptional activation. Genes Dev. 12:2153–2163.
   PubMedGoogle Scholar
• Fortini, M. E., and S. Artavanis-Tsakonas. 1994. The suppressor of hairless protein participates in Notch receptor signaling. Cell 79:273–282.
   PubMed Web of Science ®Google Scholar
• Hamaguchi, Y., Y. Yamamoto, H. Iwanari, S. Maruyama, T. Furukawa, N. Matsunami, and T. Honjo. 1992. Biochemical and immunological characterization of the DNA binding protein. (RBP-J κ) to mouse J κ recombination signal sequence. J. Biochem. (Tokyo) 112:314–320.
   PubMedGoogle Scholar
• Hsieh, J. J., T. Henkel, P. Salmon, E. Robey, M. G. Peterson, and S. D. Hayward. 1996. Truncated mammalian Notch1 activates CBF1/RBPJκ-repressed genes by a mechanism resembling that of Epstein-Barr virus EBNA2. Mol. Cell. Biol. 16:952–959.
   PubMedGoogle Scholar
• Hsieh, J. J., S. Zhou, L. Chen, D. B. Young, and S. D. Hayward. 1999. CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex. Proc. Natl. Acad. Sci. USA. 96:23–28.
   PubMed Web of Science ®Google Scholar
• Jarriault, S., C. Brou, F. Logeat, E. H. Schroeter, R. Kopan, and A. Israel. 1995. Signalling downstream of activated mammalian Notch. Nature 377:355–358.
   PubMed Web of Science ®Google Scholar
• Jarriault, S., B. O. Le, E. Hirsinger, O. Pourquie, F. Logeat, C. F. Strong, C. Brou, N. G. Seidah, and A. Israel. 1998. Delta-1 activation of notch-1 signaling results in HES-1 transactivation. Mol. Cell. Biol. 18:7423–7431.
   PubMed Web of Science ®Google Scholar
• Jeffries, S., and A. J. Capobianco. 2000. Neoplastic transformation by Notch requires nuclear localization. Mol. Cell. Biol. 20:3928–3941.
   PubMed Web of Science ®Google Scholar
• Kao, H. Y., P. Ordentlich, N. Koyano, Z. Tang, M. Downes, C. R. Kintner, R. M. Evans, and T. Kadesch. 1998. A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. Genes Dev. 12:2269–2277.
   PubMed Web of Science ®Google Scholar
• Kato, H., Y. Taniguchi, H. Kurooka, S. Minoguchi, T. Sakai, S. Nomura-Okazaki, K. Tamura, and T. Honjo. 1997. Involvement of RBP-J in biological functions of mouse Notch1 and its derivatives. Development 124:4133–4141.
   PubMedGoogle Scholar
• Kidd, S., T. Lieber, and M. W. Young. 1998. Ligand-induced cleavage and regulation of nuclear entry of Notch in Drosophila melanogaster embryos. Genes Dev. 12:3728–3740.
   PubMedGoogle Scholar
• Kopan, R., J. S. Nye, and H. Weintraub. 1994. The intracellular domain of mouse Notch: a constitutively activated repressor of myogenesis directed at the basic helix-loop-helix region of MyoD. Development 120:2385–2396.
   PubMed Web of Science ®Google Scholar
• Kornberg, R. D., and Y. Lorch. 1999. Chromatin-modifying and -remodeling complexes. Curr. Opin. Genet. Dev. 9:148–151.
   PubMed Web of Science ®Google Scholar
• Kuroda, K., S. Tani, K. Tamura, S. Minoguchi, H. Kurooka, and T. Honjo. 1999. Delta-induced Notch signaling mediated by RBP-J inhibits MyoD expression and myogenesis. J. Biol. Chem. 274:7238–7244.
   PubMed Web of Science ®Google Scholar
• Kurooka, H., and T. Honjo. 2000. Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5. J. Biol. Chem. 275:17211–17220.
   PubMed Web of Science ®Google Scholar
• Kurooka, H., K. Kuroda, and T. Honjo. 1998. Roles of the ankyrin repeats and C-terminal region of the mouse notch1 intracellular region. Nucleic Acids Res. 26:5448–5455.
   PubMed Web of Science ®Google Scholar
• Lecourtois, M., and F. Schweisguth. 1995. The neurogenic suppressor of hairless DNA-binding protein mediates the transcriptional activation of the enhancer of split complex genes triggered by Notch signaling. Genes Dev. 9:2598–2608.
   PubMed Web of Science ®Google Scholar
• Minoguchi, S., Y. Taniguchi, H. Kato, T. Okazaki, L. J. Strobl, U. ZimberStrobl, G. W. Bornkamm, and T. Honjo. 1997. RBP-L, a transcription factor related to RBP-Jκ. Mol. Cell. Biol. 17:2679–2687.
   PubMedGoogle Scholar
• Nevels, M., B. Täuber, E. Kremmer, T. Spruss, H. Wolf, and T. Dobner. 1999. Transforming potential of the adenovirus type 5 E4orf3 protein. J. Virol. 73:1591–1600.
   PubMedGoogle Scholar
• Nofziger, D., A. Miyamoto, K. M. Lyons, and G. Weinmaster. 1999. Notch signaling imposes two distinct blocks in the differentiation of C2C12 myoblasts. Development 126:1689–1702.
   PubMedGoogle Scholar
• Ohtsuka, T., M. Ishibashi, G. Gradwohl, S. Nakanishi, F. Guillemot, and R. Kageyama. 1999. Hes1 and Hes5 as notch effectors in mammalian neuronal differentiation. EMBO J. 18:2196–2207.
   PubMed Web of Science ®Google Scholar
• Olave, I., D. Reinberg, and L. D. Vales. 1998. The mammalian transcriptional repressor RBP (CBF1) targets TFIID and TFIIA to prevent activated transcription. Genes Dev. 12:1621–1637.
   PubMedGoogle Scholar
• Ordentlich, P., A. Lin, C. P. Shen, C. Blaumueller, K. Matsuno, S. Artavanis-Tsakonas, and T. Kadesch. 1998. Notch inhibition of E47 supports the existence of a novel signaling pathway. Mol. Cell. Biol. 18:2230–2239.
   PubMed Web of Science ®Google Scholar
• Oswald, F., T. Dobner, and M. Lipp. 1996. The E2F transcription factor activates a replication-dependent human H2A gene in early S-phase of the cell cycle. Mol. Cell. Biol. 16:1889–1895.
   PubMedGoogle Scholar
• Oswald, F., S. Liptay, G. Adler, and R. M. Schmid. 1998. NF-κB2 is a putative target gene of activated Notch-1 via RBP-Jκ. Mol. Cell. Biol. 18:2077–2088.
   PubMedGoogle Scholar
• Perkins, N. D., L. K. Felzien, J. C. Betts, K. Leung, D. H. Beach, and G. J. Nabel. 1997. Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator. Science 275:523–527.
   PubMed Web of Science ®Google Scholar
• Roehl, H., and J. Kimble. 1993. Control of cell fate in C. elegans by a GLP-1 peptide consisting primarily of ankyrin repeats. Nature 364:632–635.
   PubMedGoogle Scholar
• Rubenwolf, S., H. Schutt, M. Nevels, H. Wolf, and T. Dobner. 1997. Structural analysis of the adenovirus type 5 E1B 55-kilodalton-E4orf6 protein complex. J. Virol. 71:1115–1123.
   PubMedGoogle Scholar
• Schmid, R. M., S. Liptay, J. C. Betts, and G. J. Nabel. 1994. Structural and functional analysis of NF-κ B. Determinants of DNA binding specificity and protein interaction. J. Biol. Chem. 269:32162–32167.
   PubMedGoogle Scholar
• Schroeter, E. H., J. A. Kisslinger, and R. Kopan. 1998. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393:382–386.
   PubMed Web of Science ®Google Scholar
• Shawber, C., D. Nofziger, J. J. Hsieh, C. Lindsell, O. Bogler, D. Hayward, and G. Weinmaster. 1996. Notch signaling inhibits muscle cell differentiation through a CBF1-independent pathway. Development 122:3765–3773.
   PubMedGoogle Scholar
• Soutoglou, E., G. Papafotiou, N. Katrakili, and I. Talianidis. 2000. Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins. J. Biol. Chem. 275:12515–12520.
   PubMed Web of Science ®Google Scholar
• Soutoglou, E., B. Viollet, M. Vaxillaire, M. Yaniv, M. Pontoglio, and I. Talianidis. 2001. Transcription factor-dependent regulation of CBP and P/CAF histone acetyltransferase activity. EMBO J. 20:1984–1992.
   PubMed Web of Science ®Google Scholar
• Stein, R. W., M. Corrigan, P. Yaciuk, J. Whelan, and E. Moran. 1990. Analysis of E1A-mediated growth regulation functions: binding of the 300-kilodalton cellular product correlates with E1A enhancer repression function and DNA synthesis-inducing activity. J. Virol. 64:4421–4427.
   PubMedGoogle Scholar
• Struhl, G., and A. Adachi. 1998. Nuclear access and action of notch in vivo. Cell 93:649–660.
   PubMed Web of Science ®Google Scholar
• Tamura, K., Y. Taniguchi, S. Minoguchi, T. Sakai, T. Tun, T. Furukawa, and T. Honjo. 1995. Physical interaction between a novel domain of the receptor Notch and the transcription factor RBP-J κ/Su(H). Curr. Biol. 5:1416–1423.
   PubMed Web of Science ®Google Scholar
• Waltzer, L., P. Y. Bourillot, A. Sergeant, and E. Manet. 1995. RBP-J κ repression activity is mediated by a co-repressor and antagonized by the Epstein-Barr virus transcription factor EBNA2. Nucleic Acids Res. 23:4939–4945.
   PubMedGoogle Scholar
• Wang, H. G., Y. Rikitake, M. C. Carter, P. Yaciuk, S. E. Abraham, B. Zerler, and E. Moran. 1993. Identification of specific adenovirus E1A N-terminal residues critical to the binding of cellular proteins and to the control of cell growth. J. Virol. 67:476–488.
   PubMedGoogle Scholar
• Webster, G. A., and N. D. Perkins. 1999. Transcriptional cross talk between NF-κB and p53. Mol. Cell. Biol. 19:3485–3495.
   PubMed Web of Science ®Google Scholar
• Wu, L., J. C. Aster, S. C. Blacklow, R. Lake, S. Artavanis-Tsakonas, and J. D. Griffin. 2000. MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors. Nat. Genet. 26:484–489.
   PubMed Web of Science ®Google Scholar
• Yang, X. J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319–324.
   PubMed Web of Science ®Google Scholar
• Yuan, W., G. Condorelli, M. Caruso, A. Felsani, and A. Giordano. 1996. Human p300 protein is a coactivator for the transcription factor MyoD. J. Biol. Chem. 271:9009–9013.
   PubMed Web of Science ®Google Scholar