Small molecule RITA binds to p53, blocks p53–HDM-2 interaction and activates p53 function in tumors (original) (raw)

• Vogelstein, B., Lane, D. & Levine, A.J. Surfing the p53 network. Nature 408, 307–310 (2000).
  Article CAS Google Scholar
• Olivier, M. et al. The IARC TP53 database: new online mutation analysis and recommendations to users. Hum. Mutat. 19, 607–614 (2002).
  Article CAS Google Scholar
• Chene, P. Inhibiting the p53–MDM2 interaction: an important target for cancer therapy. Nat. Rev. Cancer 3, 102–109 (2003).
  Article CAS Google Scholar
• Prives, C. Signaling to p53: breaking the MDM2-p53 circuit. Cell 95, 5–8 (1998).
  Article CAS Google Scholar
• Montes de Oca Luna, R., Wagner, D.S. & Lozano, G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378, 203–206 (1995).
  Article CAS Google Scholar
• Vousden, K.H. Activation of the p53 tumor suppressor protein. Biochim. Biophys. Acta 1602, 47–59.(2002).
  CAS PubMed Google Scholar
• Evan, G. & Littlewood, T. A matter of life and cell death. Science 281, 1317–1322 (1998).
  Article CAS Google Scholar
• Bottger, A. et al. Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo. Curr. Biol. 7, 860–869 (1997).
  Article CAS Google Scholar
• Chene, P. et al. A small synthetic peptide, which inhibits the p53-hdm2 interaction, stimulates the p53 pathway in tumour cell lines. J. Mol. Biol. 299, 245–253 (2000).
  Article CAS Google Scholar
• Midgley, C.A. et al. An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 19, 2312–2323 (2000).
  Article CAS Google Scholar
• Lai, Z. et al. Differentiation of Hdm2-mediated p53 ubiquitination and Hdm2 autoubiquitination activity by small molecular weight inhibitors. Proc. Natl. Acad. Sci. USA 99, 14734–14739 (2002).
  Article CAS Google Scholar
• Zhao, J. et al. The initial evaluation of non-peptidic small-molecule HDM2 inhibitors based on p53–HDM2 complex structure. Cancer Lett. 183, 69–77 (2002).
  Article CAS Google Scholar
• Vassilev, L.T. et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 303, 844–848 (2004).
  Article CAS Google Scholar
• Bunz, F. et al. Requirement for p53 and p21 to sustain G2 arrest after DNA damage. Science 282, 1497–1501 (1998).
  Article CAS Google Scholar
• Bunz, F. et al. Disruption of p53 in human cancer cells alters the responses to therapeutic agents. J. Clin. Invest. 104, 263–269 (1999).
  Article CAS Google Scholar
• Rigler, R. et al. Specific binding of proinsulin C-peptide to human cell membranes. Proc. Natl. Acad. Sci. USA 96, 13318–13323 (1999).
  Article CAS Google Scholar
• Yakovleva, T. et al. p53 Latency. C-terminal domain prevents binding of p53 core to target but not to nonspecific DNA sequences. J. Biol. Chem. 276, 15650–15658 (2001).
  Article CAS Google Scholar
• Wang, L., Grossman, S.R. & Kieff, E. Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter. Proc. Natl. Acad. Sci. USA 97, 430–435 (2000).
  Article CAS Google Scholar
• Lin, J., Chen, J., Elenbaas, B. & Levine, A.J. Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kDa protein. Genes Dev. 8, 1235–1246 (1994).
  Article CAS Google Scholar
• Kussie, P.H. et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274, 948–953. (1996).
  Article CAS Google Scholar
• Burch, L.R., Midgley, C.A., Currie, R.A., Lane, D.P. & Hupp, T.R. Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA. FEBS Lett. 472, 93–98 (2000).
  Article CAS Google Scholar
• Kanovsky, M. et al. Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells. Proc. Natl. Acad. Sci. USA 98, 12438–12443 (2001).
  Article CAS Google Scholar
• Gu, W. & Roeder, R.G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595–606 (1997).
  Article CAS Google Scholar
• Grossman, S.R. et al. Polyubiquitination of p53 by a ubiquitin ligase activity of p300. Science 300, 342–344 (2003).
  Article CAS Google Scholar
• Bergamaschi, D. et al. iASPP oncoprotein is a key inhibitor of p53 conserved from worm to human. Nat. Genet. 33, 162–167 (2003).
  Article CAS Google Scholar
• Mihara, M. et al. p53 has a direct apoptogenic role at the mitochondria. Mol. Cell 11, 577–590 (2003).
  Article CAS Google Scholar
• Nikolaev, A.Y., Li, M., Puskas, N., Qin, J. & Gu, W. Parc: a cytoplasmic anchor for p53. Cell 112, 29–40 (2003).
  Article CAS Google Scholar
• Pandhare, J., Dash, C., Rao, M. & Deshpande, V. Slow tight binding inhibition of proteinase K by a proteinaceous inhibitor: conformational alterations responsible for conferring irreversibility to the enzyme-inhibitor complex. J. Biol. Chem. 278, 48735–48744 (2003).
  Article CAS Google Scholar
• Jabbur, J.R. et al. Mdm-2 binding and TAF(II)31 recruitment is regulated by hydrogen bond disruption between the p53 residues Thr18 and Asp21. Oncogene 21, 7100–7113 (2002).
  Article CAS Google Scholar
• Iyer, N.G. et al. p300 regulates p53-dependent apoptosis after DNA damage in colorectal cancer cells by modulation of PUMA/p21 levels. Proc. Natl. Acad. Sci. USA 101, 7386–7391 (2004).
  Article CAS Google Scholar
• Grossman, S.R. et al. p300/MDM2 complexes participate in MDM2-mediated p53 degradation. Mol. Cell 2, 405–415 (1998).
  Article CAS Google Scholar
• Liu, W.L., Midgley, C., Stephen, C., Saville, M. & Lane, D.P. Biological significance of a small highly conserved region in the N terminus of the p53 tumour suppressor protein. J. Mol. Biol. 313, 711–731 (2001).
  Article CAS Google Scholar
• Friedlander, P., Legros, Y., Soussi, T. & Prives, C. Regulation of mutant p53 temperature-sensitive DNA binding. J. Biol. Chem. 271, 25468–25478 (1996).
  Article CAS Google Scholar
• Hansen, S., Hupp, T.R. & Lane, D.P. Allosteric regulation of the thermostability and DNA binding activity of human p53 by specific interacting proteins. CRC Cell Transformation Group. J. Biol. Chem. 271, 3917–3924 (1996).
  Article CAS Google Scholar
• Cho, Y., Gorina, S., Jeffrey, P.D. & Pavletich, N.P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265, 346–355 (1994).
  Article CAS Google Scholar
• Jeffrey, P.D., Gorina, S. & Pavletich, N.P. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science 267, 1498–14502 (1995).
  Article CAS Google Scholar
• Lee, W. et al. Solution structure of the tetrameric minimum transforming domain of p53. Nat. Struct. Biol. 1, 877–890 (1994).
  Article CAS Google Scholar
• Baker, S.J., Markowitz, S., Fearon, E.R., Willson, J.K. & Vogelstein, B. Suppression of human colorectal carcinoma cell growth by wild-type p53. Science 249, 912–915 (1990).
  Article CAS Google Scholar
• D'Orazi, G. et al. Exogenous wt-p53 protein is active in transformed cells but not in their non-transformed counterparts: implications for cancer gene therapy without tumor targeting. J. Gene Med. 2, 11–21 (2000).
  Article CAS Google Scholar
• Nieves-Neira, W. et al. DNA protein cross-links produced by NSC 652287, a novel thiophene derivative active against human renal cancer cells. Mol. Pharmacol. 56, 478–484 (1999).
  Article CAS Google Scholar
• Rivera, M.I. et al. Selective toxicity of the tricyclic thiophene NSC 652287 in renal carcinoma cell lines: differential accumulation and metabolism. Biochem. Pharmacol. 57, 1283–1295 (1999).
  Article CAS Google Scholar
• Selivanova, G. et al. The single-stranded DNA end binding site of p53 coincides with the C- terminal regulatory region. Nucleic Acids Res. 24, 3560–3567 (1996).
  Article CAS Google Scholar
• Schuhmacher, M. et al. Control of cell growth by c-Myc in the absence of cell division. Curr. Biol. 9, 1255–1258 (1999).
  Article CAS Google Scholar
• Felsher, D.W. & Bishop, J.M. Transient excess of MYC activity can elicit genomic instability and tumorigenesis. Proc. Natl. Acad. Sci. USA 96, 3940–3944 (1999).
  Article CAS Google Scholar
• Vigo, E. et al. CDC25A phosphatase is a target of E2F and is required for efficient E2F-induced S phase. Mol. Cell. Biol. 19, 6379–6395 (1999).
  Article CAS Google Scholar
• Hengstermann, A., Linares, L.K., Ciechanover, A., Whitaker, N.J. & Scheffner, M. Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cells. Proc. Natl. Acad. Sci. USA 98, 1218–1223 (2001).
  Article CAS Google Scholar