Making sense of ubiquitin ligases that regulate p53

References

• Soussi T, Beroud C. Assessing TP53 status in human tumours to evaluate clinical outcome. Nat Rev Cancer 2001; 1:233 - 240
   PubMed Web of Science ®Google Scholar
• Hainaut P, Hollstein M. p53 and human cancer: The first ten thousand mutations. Adv Cancer Res 2000; 77:81 - 137
   PubMed Web of Science ®Google Scholar
• Vousden KH, Prives C. Blinded by the Light: The Growing Complexity of p53. Cell 2009; 137:413 - 431
   PubMed Web of Science ®Google Scholar
• Loewer A, Batchelor E, Gaglia G, Lahav G. Basal dynamics of p53 reveal transcriptionally attenuated pulses in cycling cells. Cell 142:89 - 100
   PubMed Web of Science ®Google Scholar
• Hu W, Chan CS, Wu R, Zhang C, Sun Y, Song JS, et al. Negative Regulation of Tumor Suppressor p53 by MicroRNA miR-504. Mol Cell 38:689 - 699
   PubMed Web of Science ®Google Scholar
• Vogelstein B, Lane D, Levine AJ. Surfing the p53 network. Nature 2000; 408:307 - 310
   PubMed Web of Science ®Google Scholar
• Horn HF, Vousden KH. Coping with stress: multiple ways to activate p53. Oncogene 2007; 26:1306 - 1316
   PubMed Web of Science ®Google Scholar
• Riley T, Sontag E, Chen P, Levine A. Transcriptional control of human p53-regulated genes. Nat Rev Mol Cell Biol 2008; 9:402 - 412
   PubMed Web of Science ®Google Scholar
• Laptenko O, Prives C. Transcriptional regulation by p53: one protein, many possibilities. Cell Death Differ 2006; 13:951 - 961
   PubMed Web of Science ®Google Scholar
• Carter S, Vousden KH. Modifications of p53: competing for the lysines. Curr Opin Genet Dev 2009; 19:18 - 24
   PubMed Web of Science ®Google Scholar
• Kruse JP, Gu W. Modes of p53 regulation. Cell 2009; 137:609 - 622
   PubMed Web of Science ®Google Scholar
• Deshaies RJ, Joazeiro CA. RING domain E3 ubiquitin ligases. Annu Rev Biochem 2009; 78:399 - 434
   PubMed Web of Science ®Google Scholar
• Chen ZJ, Sun LJ. Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell 2009; 33:275 - 286
   PubMed Web of Science ®Google Scholar
• Brooks CL, Gu W. p53 ubiquitination: Mdm2 and beyond. Mol Cell 2006; 21:307 - 315
   PubMed Web of Science ®Google Scholar
• Mukhopadhyay D, Riezman H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007; 315:201 - 205
   PubMed Web of Science ®Google Scholar
• Jain AK, Barton MC. Regulation of p53: TRIM24 enters the RING. Cell Cycle 2009; 8:3668 - 3674
   PubMed Web of Science ®Google Scholar
• Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997; 387:296 - 299
   PubMed Web of Science ®Google Scholar
• Honda R, Tanaka H, Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 1997; 420:25 - 27
   PubMed Web of Science ®Google Scholar
• Kubbutat MH, Jones SN, Vousden KH. Regulation of p53 stability by Mdm2. Nature 1997; 387:299 - 303
   PubMed Web of Science ®Google Scholar
• Jones SN, Roe AE, Donehower LA, Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 1995; 378:206 - 208
   PubMed Web of Science ®Google Scholar
• Montes de Oca Luna R, Wagner DS, Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 1995; 378:203 - 206
   PubMed Web of Science ®Google Scholar
• Lu WJ, Abrams JM. Lessons from p53 in non-mammalian models. Cell Death Differ 2006; 13:909 - 912
   PubMed Web of Science ®Google Scholar
• Wu X, Bayle JH, Olson D, Levine AJ. The p53-mdm-2 autoregulatory feedback loop. Genes Dev 1993; 7:1126 - 1132
   PubMed Web of Science ®Google Scholar
• Stommel JM, Wahl GM. Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation. EMBO J 2004; 23:1547 - 1556
   PubMed Web of Science ®Google Scholar
• Manfredi JJ. The Mdm2-p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor. Genes Dev 24:1580 - 1589
   PubMed Web of Science ®Google Scholar
• Momand J, Zambetti GP, Olson DC, George D, Levine AJ. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 1992; 69:1237 - 1245
   PubMed Web of Science ®Google Scholar
• Chen J, Marechal V, Levine AJ. Mapping of the p53 and mdm-2 interaction domains. Mol Cell Biol 1993; 13:4107 - 4114
   PubMed Web of Science ®Google Scholar
• Yu GW, Rudiger S, Veprintsev D, Freund S, Fernandez-Fernandez MR, Fersht AR. The central region of HDM2 provides a second binding site for p53. Proc Natl Acad Sci USA 2006; 103:1227 - 1232
   PubMed Web of Science ®Google Scholar
• Shimizu H, Burch LR, Smith AJ, Dornan D, Wallace M, Ball KL, Hupp TR. The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo. J Biol Chem 2002; 277:28446 - 28458
   PubMed Web of Science ®Google Scholar
• Marine JC, Francoz S, Maetens M, Wahl G, Toledo F, Lozano G. Keeping p53 in check: essential and synergistic functions of Mdm2 and Mdm4. Cell Death Differ 2006; 13:927 - 934
   PubMed Web of Science ®Google Scholar
• Uldrijan S, Pannekoek WJ, Vousden KH. An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. EMBO J 2007; 26:102 - 112
   PubMed Web of Science ®Google Scholar
• Singh RK, Iyappan S, Scheffner M. Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2. J Biol Chem 2007; 282:10901 - 10907
   PubMed Web of Science ®Google Scholar
• Meek DW, Knippschild U. Posttranslational modification of MDM2. Mol Cancer Res 2003; 1:1017 - 1026
   PubMed Web of Science ®Google Scholar
• Kawai H, Wiederschain D, Kitao H, Stuart J, Tsai KK, Yuan ZM. DNA damage-induced MDMX degradation is mediated by MDM2. J Biol Chem 2003; 278:45946 - 45953
   PubMed Web of Science ®Google Scholar
• Li M, Brooks CL, Wu-Baer F, Chen D, Baer R, Gu W. Mono- versus poly-ubiquitination: differential control of p53 fate by Mdm2. Science 2003; 302:1972 - 1975
   PubMed Web of Science ®Google Scholar
• Nie L, Sasaki M, Maki CG. Regulation of p53 nuclear export through sequential changes in conformation and ubiquitination. J Biol Chem 2007; 282:14616 - 14625
   PubMed Web of Science ®Google Scholar
• Grossman SR, Deato ME, Brignone C, Chan HM, Kung AL, Tagami H, et al. Polyubiquitination of p53 by a ubiquitin ligase activity of p300. Science 2003; 300:342 - 344
   PubMed Web of Science ®Google Scholar
• Sui G, Affar el B, Shi Y, Brignone C, Wall NR, Yin P, et al. Yin Yang 1 is a negative regulator of p53. Cell 2004; 117:859 - 872
   PubMed Web of Science ®Google Scholar
• Higashitsuji H, Itoh K, Sakurai T, Nagao T, Sumitomo Y, Masuda T, et al. The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation and degradation of p53. Cancer Cell 2005; 8:75 - 87
   PubMed Web of Science ®Google Scholar
• Wang C, Ivanov A, Chen L, Fredericks WJ, Seto E, Rauscher FJ 3rd, Chen J. MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation. EMBO J 2005; 24:3279 - 3290
   PubMed Web of Science ®Google Scholar
• Du W, Jiang P, Li N, Mei Y, Wang X, Wen L, et al. Suppression of p53 activity by Siva1. Cell Death Differ 2009; 16:1493 - 1504
   PubMed Web of Science ®Google Scholar
• Xirodimas DP, Saville MK, Bourdon JC, Hay RT, Lane DP. Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity. Cell 2004; 118:83 - 97
   PubMed Web of Science ®Google Scholar
• Carter S, Bischof O, Dejean A, Vousden KH. C-terminal modifications regulate MDM2 dissociation and nuclear export of p53. Nat Cell Biol 2007; 9:428 - 435
   PubMed Web of Science ®Google Scholar
• Tang Y, Zhao W, Chen Y, Zhao Y, Gu W. Acetylation is indispensable for p53 activation. Cell 2008; 133:612 - 626
   PubMed Web of Science ®Google Scholar
• Itahana K, Mao H, Jin A, Itahana Y, Clegg HV, Lindstrom MS, et al. Targeted inactivation of Mdm2 RING finger E3 ubiquitin ligase activity in the mouse reveals mechanistic insights into p53 regulation. Cancer Cell 2007; 12:355 - 366
   PubMed Web of Science ®Google Scholar
• Ringshausen I, O'Shea CC, Finch AJ, Swigart LB, Evan GI. Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo. Cancer Cell 2006; 10:501 - 514
   PubMed Web of Science ®Google Scholar
• Feng L, Lin T, Uranishi H, Gu W, Xu Y. Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity. Mol Cell Biol 2005; 25:5389 - 5395
   PubMed Web of Science ®Google Scholar
• Krummel KA, Lee CJ, Toledo F, Wahl GM. The C-terminal lysines fine-tune p53 stress responses in a mouse model but are not required for stability control or transactivation. Proc Natl Acad Sci USA 2005; 102:10188 - 10193
   PubMed Web of Science ®Google Scholar
• Leng RP, Lin Y, Ma W, Wu H, Lemmers B, Chung S, et al. Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 2003; 112:779 - 791
   PubMed Web of Science ®Google Scholar
• Parant J, Chavez-Reyes A, Little NA, Yan W, Reinke V, Jochemsen AG, Lozano G. Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. Nat Genet 2001; 29:92 - 95
   PubMed Web of Science ®Google Scholar
• Daujat S, Neel H, Piette J. Preferential expression of Mdm2 oncogene during the development of neural crest and its derivatives in mouse early embryogenesis. Mech Dev 2001; 103:163 - 165
   PubMed Web of Science ®Google Scholar
• Chavez-Reyes A, Parant JM, Amelse LL, de Oca Luna RM, Korsmeyer SJ, Lozano G. Switching mechanisms of cell death in mdm2- and mdm4-null mice by deletion of p53 downstream targets. Cancer Res 2003; 63:8664 - 8669
   PubMed Web of Science ®Google Scholar
• Bourdon JC. p53 and its isoforms in cancer. Br J Cancer 2007; 97:277 - 282
   PubMed Web of Science ®Google Scholar
• Midgley CA, Owens B, Briscoe CV, Thomas DB, Lane DP, Hall PA. Coupling between gamma irradiation, p53 induction and the apoptotic response depends upon cell type in vivo. J Cell Sci 1995; 108:1843 - 1848
   PubMed Web of Science ®Google Scholar
• Terzian T, Suh YA, Iwakuma T, Post SM, Neumann M, Lang GA, et al. The inherent instability of mutant p53 is alleviated by Mdm2 or p16INK4a loss. Genes Dev 2008; 22:1337 - 1344
   PubMed Web of Science ®Google Scholar
• Laine A, Topisirovic I, Zhai D, Reed JC, Borden KL, Ronai Z. Regulation of p53 localization and activity by Ubc13. Mol Cell Biol 2006; 26:8901 - 8913
   PubMed Web of Science ®Google Scholar
• Khetchoumian K, Teletin M, Tisserand J, Mark M, Herquel B, Ignat M, et al. Loss of Trim24 (Tif1alpha) gene function confers oncogenic activity to retinoic acid receptor alpha. Nat Genet 2007; 39:1500 - 1506
   PubMed Web of Science ®Google Scholar
• Allton K, Jain AK, Herz HM, Tsai WW, Jung SY, Qin J, et al. Trim24 targets endogenous p53 for degradation. Proc Natl Acad Sci USA 2009; 106:11612 - 11616
   PubMed Web of Science ®Google Scholar
• Liu L, Scolnick DM, Trievel RC, Zhang HB, Marmorstein R, Halazonetis TD, Berger SL. p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol Cell Biol 1999; 19:1202 - 1209
   PubMed Web of Science ®Google Scholar
• Huang J, Perez-Burgos L, Placek BJ, Sengupta R, Richter M, Dorsey JA, et al. Repression of p53 activity by Smyd2-mediated methylation. Nature 2006; 444:629 - 632
   PubMed Web of Science ®Google Scholar
• Huang J, Sengupta R, Espejo AB, Lee MG, Dorsey JA, Richter M, et al. p53 is regulated by the lysine demethylase LSD1. Nature 2007; 449:105 - 108
   PubMed Web of Science ®Google Scholar
• Huang J, Dorsey J, Chuikov S, Perez-Burgos L, Zhang X, Jenuwein T, et al. G9a and Glp methylate lysine 373 in the tumor suppressor p53. J Biol Chem 285 9636 9641
   Web of Science ®Google Scholar
• Murray-Zmijewski F, Slee EA, Lu X. A complex barcode underlies the heterogeneous response of p53 to stress. Nat Rev Mol Cell Biol 2008; 9:702 - 712
   PubMed Web of Science ®Google Scholar
• Bode AM, Dong Z. Post-translational modification of p53 in tumorigenesis. Nat Rev Cancer 2004; 4:793 - 805
   PubMed Web of Science ®Google Scholar
• Olsson A, Manzl C, Strasser A, Villunger A. How important are post-translational modifications in p53 for selectivity in target-gene transcription and tumour suppression?. Cell Death Differ 2007; 14:1561 - 1575
   PubMed Web of Science ®Google Scholar
• Toledo F, Wahl GM. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nat Rev Cancer 2006; 6:909 - 923
   PubMed Web of Science ®Google Scholar
• Yang WH, Kim JE, Nam HW, Ju JW, Kim HS, Kim YS, Cho JW. Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat Cell Biol 2006; 8:1074 - 1083
   PubMed Web of Science ®Google Scholar
• Meek DW, Anderson CW. Posttranslational Modification of p53: cooperative integrators of function. Cold Spring Harb Perspect Biol 2009; 1:000950
   PubMed Web of Science ®Google Scholar
• Harris SL, Levine AJ. The p53 pathway: positive and negative feedback loops. Oncogene 2005; 24:2899 - 2908
   PubMed Web of Science ®Google Scholar
• Donehower LA, Lozano G. 20 years studying p53 functions in genetically engineered mice. Nat Rev Cancer 2009; 9:831 - 841
   PubMed Web of Science ®Google Scholar
• Shi D, Pop MS, Kulikov R, Love IM, Kung AL, Grossman SR. CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53. Proc Natl Acad Sci USA 2009; 106:16275 - 16280
   PubMed Web of Science ®Google Scholar
• Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997; 90:595 - 606
   PubMed Web of Science ®Google Scholar
• Sato Y, Kamura T, Shirata N, Murata T, Kudoh A, Iwahori S, et al. Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex. PLoS Pathog 2009; 5:1000530
   Web of Science ®Google Scholar
• Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S. Molecular basis of Pirh2-mediated p53 ubiquitylation. Nat Struct Mol Biol 2008; 15:1334 - 1342
   PubMed Web of Science ®Google Scholar
• Dornan D, Wertz I, Shimizu H, Arnott D, Frantz GD, Dowd P, et al. The ubiquitin ligase COP1 is a critical negative regulator of p53. Nature 2004; 429:86 - 92
   PubMed Web of Science ®Google Scholar
• Rajendra R, Malegaonkar D, Pungaliya P, Marshall H, Rasheed Z, Brownell J, et al. Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53. J Biol Chem 2004; 279:36440 - 36444
   PubMed Web of Science ®Google Scholar
• Chen D, Kon N, Li M, Zhang W, Qin J, Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 2005; 121:1071 - 1083
   PubMed Web of Science ®Google Scholar
• Laine A, Ronai Z. Regulation of p53 localization and transcription by the HECT domain E3 ligase WWP1. Oncogene 2007; 26:1477 - 1483
   PubMed Web of Science ®Google Scholar
• Boutell C, Everett RD. The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and Ubiquitinates p53. J Biol Chem 2003; 278:36596 - 36602
   PubMed Web of Science ®Google Scholar
• Andrews P, He YJ, Xiong Y. Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing p53 function. Oncogene 2006; 25:4534 - 4548
   PubMed Web of Science ®Google Scholar
• Yang W, Rozan LM, McDonald ER 3rd, Navaraj A, Liu JJ, Matthew EM, et al. CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation. J Biol Chem 2007; 282:3273 - 3281
   PubMed Web of Science ®Google Scholar
• Yamasaki S, Yagishita N, Sasaki T, Nakazawa M, Kato Y, Yamadera T, et al. Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase ‘Synoviolin’. EMBO J 2007; 26:113 - 122
   PubMed Web of Science ®Google Scholar
• Esser C, Scheffner M, Hohfeld J. The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J Biol Chem 2005; 280:27443 - 27448
   PubMed Web of Science ®Google Scholar
• Le Cam L, Linares LK, Paul C, Julien E, Lacroix M, Hatchi E, et al. E4F1 is an atypical ubiquitin ligase that modulates p53 effector functions independently of degradation. Cell 2006; 127:775 - 788
   PubMed Web of Science ®Google Scholar
• Querido E, Blanchette P, Yan Q, Kamura T, Morrison M, Boivin D, et al. Degradation of p53 by adenovirus E4orf6 and E1B55K proteins occurs via a novel mechanism involving a Cullin-containing complex. Genes Dev 2001; 15:3104 - 3117
   PubMed Web of Science ®Google Scholar
• Kruse JP, Gu W. MSL2 promotes Mdm2-independent cytoplasmic localization of p53. J Biol Chem 2009; 284:3250 - 3263
   PubMed Web of Science ®Google Scholar
• Sun L, Shi L, Li W, Yu W, Liang J, Zhang H, et al. JFK, a Kelch domain-containing F-box protein, links the SCF complex to p53 regulation. Proc Natl Acad Sci USA 2009; 106:10195 - 10200
   PubMed Web of Science ®Google Scholar
• Lee EW, Lee MS, Camus S, Ghim J, Yang MR, Oh W, et al. Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell cycle arrest and apoptosis. EMBO J 2009; 28:2100 - 2113
   PubMed Web of Science ®Google Scholar