Regulation of p53 Function and Stability by Phosphorylation

REFERENCES

• Banin, S., L. Moyal, S.-Y. Shieh, Y. Taya, C. W. Anderson, L. Chessa, N. I. Smorodinsky, C. Prives, Y. Reiss, Y. Shiloh, and J. Ziv 1998. Enhanced phosphorylation of p53 by ATM in response to DNA damage. Science 281:1674–1677.
   PubMed Web of Science ®Google Scholar
• Banks, L., G. Matlashewski, and J. Crawford 1986. Isolation of human p53 specific monoclonal antibodies and their use in the studies of human p53 expression. Eur. J. Biochem. 159:529–534.
   PubMedGoogle Scholar
• Bates, S., and J. Vousden 1996. p53 in signalling checkpoint arrest or apoptosis. Curr. Opin. Genet. Dev. 6:1–7.
   PubMedGoogle Scholar
• Blaydes, J. P., and J. Hupp 1998. DNA damage triggers DRB-resistant phosphorylation of human p53 at the CK2 site. Oncogene 17:1045–1052.
   PubMed Web of Science ®Google Scholar
• Böttger, A., V. Böttger, A. Sparks, L. W.-L., S. F. Howard, and J. Lane 1997. Design of a synthetic Mdm2 binding mini protein that activates the p53 response in vivo. Curr. Biol. 7:860–869.
   PubMed Web of Science ®Google Scholar
• Canman, C. E., D.-S. Lim, K. A. Cimprich, Y. Taya, K. Tamai, K. Sakaguchi, E. Appella, M. B. Kastan, and J. Siliciano 1998. Activation of the ATM kinase by ionizing radiation and phosphorylation of p53. Science 281:1677–1679.
   PubMed Web of Science ®Google Scholar
• Crook, T., N. J. Marston, E. A. Sara, and J. Vousden 1994. Transcriptional activation by p53 correlates with suppression of growth but not transformation. Cell 79:817–827.
   PubMedGoogle Scholar
• El-Deiry, W., T. Tokino, V. E. Velculescu, D. B. Levy, V. E. Parson, J. M. Trent, D. Lin, W. E. Mercer, K. W. Kinzler, and J. Vogelstein 1993. WAF1, a potential mediator of p53 tumour suppression. Cell 75:817–825.
   PubMed Web of Science ®Google Scholar
• Fiscella, M., S. J. Ullrich, N. Zambrano, M. T. Shields, D. Lin, S. P. Lees-Miller, C. W. Anderson, W. E. Mercer, and J. Appella 1993. Mutation of the serine 15 phosphorylation site of human p53 reduces the ability of p53 to inhibit cell cycle progression. Oncogene 8:1519–1528.
   PubMedGoogle Scholar
• Fiscella, M., N. Zambrano, S. J. Ullrich, T. Unger, D. Lin, B. Cho, W. E. Mercer, C. W. Anderson, and J. Appella 1994. The carboxy-terminal serine 392 phosphorylation site of human p53 is not required for wild-type activities. Oncogene 9:3249–3257.
   PubMed Web of Science ®Google Scholar
• Friedlander, P., Y. Haupt, C. Prives, and J. Oren 1996. A mutant p53 that discriminated between p53-responsive genes cannot induce apoptosis. Mol. Cell. Biol. 16:4961–4971.
   PubMed Web of Science ®Google Scholar
• Fuchs, B., D. O’Connor, L. Fallis, K. H. Scheidtmann, and J. Lu 1995. p53 phosphorylation mutants retain transcription activity. Oncogene 10:789–793.
   PubMedGoogle Scholar
• Fuchs, S. Y., V. Adler, T. Buschmann, Z. Yin, X. Wu, S. N. Jones, and J. Ronai 1998. JNK targets p53 ubiquitination and degradation in nonstressed cells. Genes Dev. 12:2658–2663.
   PubMed Web of Science ®Google Scholar
• Fuchs, S. Y., V. Adler, M. R. Pincus, and J. Ronai 1998. MEKK1/JNK signaling stabilizes and activates p53. Proc. Natl. Acad. Sci. USA 95:10541–10546.
   PubMed Web of Science ®Google Scholar
• Gu, W., and J. Roeder 1997. Activation of p53 sequence-specific DNA binding by acetylation of the C-terminal domain. Cell 90:595–606.
   PubMed Web of Science ®Google Scholar
• Halazonetis, T. D., and J. Kandil 1993. Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants. EMBO J. 12:5057–5064.
   PubMedGoogle Scholar
• Hao, M., A. M. Lowy, M. Kapoor, A. Deffie, G. Liu, and J. Lozano 1996. Mutation of phosphoserine 389 affects p53 function in vivo. J. Biol. Chem. 271:29380–29385.
   PubMedGoogle Scholar
• Haupt, Y., Y. Barak, and J. Oren 1996. Cell type-specific inhibition of p53-mediated apoptosis by mdm2. EMBO J. 15:1596–1606.
   PubMed Web of Science ®Google Scholar
• Haupt, Y., R. Maya, A. Kazaz, and J. Oren 1997. Mdm2 promotes the rapid degradation of p53. Nature 387:296–299.
   PubMed Web of Science ®Google Scholar
• Hupp, T. R., D. W. Meek, C. A. Midgley, and J. Lane 1992. Regulation of the specific DNA binding function of p53. Cell 71:875–886.
   PubMed Web of Science ®Google Scholar
• Juven, T., Y. Barak, A. Zauberman, D. L. George, and J. Oren 1993. Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene. Oncogene 8:3411–3416.
   PubMed Web of Science ®Google Scholar
• Kamijo, T., J. D. Weber, G. Zambetti, F. Zindy, M. F. Roussel, and J. Sherr 1998. Functional and physical interactions of the ARF tumor suppressor with p53 and Mdm2. Proc. Natl. Acad. Sci. USA 95:8292–8297.
   PubMed Web of Science ®Google Scholar
• Kapoor, M., and J. Lozano 1998. Functional activation of p53 via phosphorylation following DNA damage by UV but not γ-irradiation. Proc. Natl. Acad. Sci. USA 95:2834–2837.
   PubMed Web of Science ®Google Scholar
• Kubbutat, M. H. G., S. N. Jones, and J. Vousden 1997. Regulation of p53 stability by Mdm2. Nature 387:299–303.
   PubMed Web of Science ®Google Scholar
• Kubbutat, M. H. G., R. L. Ludwig, M. Ashcroft, and J. Vousden 1998. Regulation of Mdm2 directed degradation by the C-terminus of p53. Mol. Cell. Biol. 18:5690–5698.
   PubMed Web of Science ®Google Scholar
• Kubbutat, M. H. G., and J. Vousden 1998. Keeping an old friend under control: regulation of p53 stability. Mol. Med. Today 4:250–256.
   PubMedGoogle Scholar
• Lechner, M. S., D. H. Mack, A. B. Finicle, T. Crook, K. H. Vousden, and J. Laimins 1992. Human papillomavirus E6 proteins bind p53 in vivo and abrogate p53-mediated repression of transcription. EMBO J. 11:3045–3052.
   PubMed Web of Science ®Google Scholar
• Levine, A. J. 1997. p53, the cellular gatekeeper for growth and division. Cell 88:323–331.
   PubMed Web of Science ®Google Scholar
• Lohrum, M., and J. Scheidtmann 1996. Differential effects of phosphorylation of rat p53 on transactivation of promoters derived from different p53 responsive genes. Oncogene 13:2527–2539.
   PubMedGoogle Scholar
• Marston, N. J., T. Crook, and J. Vousden 1994. Interaction of p53 with MDM2 is independent of E6 and does not mediate wild type transformation suppressor function. Oncogene 9:2707–2716.
   PubMedGoogle Scholar
• Marston, N. J., J. R. Jenkins, and J. Vousden 1995. Oligomerisation of full length p53 contributes to the interaction with mdm2 but not HPV E6. Oncogene 10:1709–1715.
   PubMedGoogle Scholar
• Mayr, G. A., M. Reed, P. Wang, Y. Wang, J. F. Schwedes, and J. Tegtmeyer 1995. Serine phosphorylation in the NH2 terminus of p53 facilitates transactivation. Cancer Res. 55:2410–2417.
   PubMedGoogle Scholar
• Meek, D. W. 1998. Multisite phosphorylation and the integration of stress signals at p53. Cell. Signall. 10:159–166.
   PubMed Web of Science ®Google Scholar
• Meek, D. W. 1994. Post-translational modification of p53. Semin. Cancer Biol. 5:203–210.
   PubMed Web of Science ®Google Scholar
• Midgley, C. A., and J. Lane 1997. p53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding. Oncogene 15:1179–1189.
   PubMed Web of Science ®Google Scholar
• Milczarek, G. J., J. Martinez, and J. Bowden 1997. p53 phosphorylation: biochemical and functional consequences. Life Sci. 60:1–11.
   PubMedGoogle Scholar
• Milne, D. M., R. H. Palmer, and J. Meek 1992. Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53. Nucleic Acids Res. 20:5565–5570.
   PubMedGoogle Scholar
• Pise-Masison, C., M. Radonovich, K. Sakaguchi, E. Appella, and J. Brady 1998. Phosphorylation of p53: a novel pathway for p53 inactivation in human T-cell lymphotropic virus type 1-transformed cells. J. Virol. 72:6348–6355.
   PubMed Web of Science ®Google Scholar
• Pomerantz, J., N. Schreiber-Agus, N. J. Liégeois, A. Silverman, L. Alland, L. Chin, J. Potes, K. Chen, I. Orlow, H.-W. Lee, C. Cordon-Cardo, and J. DePinho 1998. The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2’s inhibition of p53. Cell 92:713–723.
   PubMed Web of Science ®Google Scholar
• Prives, C. 1998. Signaling to p53: breaking the MDM2-p53 circuit. Cell 95:5–8.
   PubMed Web of Science ®Google Scholar
• Rowan, S., R. L. Ludwig, Y. Haupt, S. Bates, X. Lu, M. Oren, and J. Vousden 1996. Specific loss of apoptotic but not cell cycle arrest function in a human tumour derived p53 mutant. EMBO J. 15:827–838.
   PubMed Web of Science ®Google Scholar
• Ryan, K. M., and J. Vousden 1998. Characterization of structural p53 mutants which show selective defects in apoptosis but not cell cycle arrest. Mol. Cell. Biol. 18:3692–3698.
   PubMed Web of Science ®Google Scholar
• Sakaguchi, K., J. E. Herrera, S. Saito, T. Miki, M. Bustin, A. Vassilev, C. W. Anderson, and J. Appella 1998. DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev. 12:2831–2841.
   PubMed Web of Science ®Google Scholar
• Shaw, P., J. Freeman, R. Bovey, and J. Iggo 1996. Regulation of specific DNA binding by p53: evidence for a role of O-glycosylation and charged residues at the carboxy-terminus. Oncogene 12:921–930.
   PubMedGoogle Scholar
• Shieh, S.-Y., M. Ikeda, Y. Taya, and J. Prives 1997. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91:325–334.
   PubMed Web of Science ®Google Scholar
• Siliciano, J. D., C. E. Canman, Y. Taya, K. Sakaguchi, E. Appella, and J. Kastan 1997. DNA damage induces phosphorylation of the amino terminus of p53. Genes Dev. 11:3471–3481.
   PubMed Web of Science ®Google Scholar
• Stott, F., S. A. Bates, M. James, B. B. McConnell, M. Starborg, S. Brookes, I. Palmero, E. Hara, K. M. Ryan, K. H. Vousden, and J. Peters 1998. The alternative product from the human CDKN2A locus, p14ARF, participates in a regulatory feedback loop with p53 and MDM2. EMBO J. 17:5001–5014.
   PubMed Web of Science ®Google Scholar
• Vojtesek, B., J. Bartek, C. A. Midgley, and J. Lane 1992. An immunochemical analysis of the human nuclear phosphoprotein p53. J. Immunol. Methods 151:237–244.
   PubMed Web of Science ®Google Scholar
• Waterman, M. J., E. S. Stavridi, J. L. Waterman, and J. Halazonetis 1998. ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins. Nat. Genet. 19:175–178.
   PubMed Web of Science ®Google Scholar