p53 regulation by ubiquitin

Brooks, Christopher L.; Gu, Wei

doi:10.1016/j.febslet.2011.05.022

Cited by 187Ubiquitin and proteasome pathwaysCancer-related Molecular PathwaysTGF-β signaling in diseases

p53 regulation by ubiquitin

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Brooks, Christopher L., Gu, Wei·2011·FEBS Letters

DOI 10.1016/j.febslet.2011.05.022PMC PMC3172401

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Abstract

The ubiquitination pathway is a highly dynamic and coordinated process that regulates degradation as well as numerous processes of proteins within a cell. The p53 tumor suppressor and several factors in the pathway are regulated by ubiquitin as well as ubiquitin-like proteins. These modifications are critical for the function of p53 and control both the degradation of the protein as well as localization and activity. Importantly, more recent studies have identified deubiquitination enzymes that can specifically remove ubiquitin moieties from p53 or other factors in the pathway, and the reversible nature of this process adds yet another layer of regulatory control of p53. This review highlights the recent advances in our knowledge of ubiquitin and the p53 pathway.

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Mdm2 functions as an E3 ubiquitin ligase that conjugates ubiquitin to proteins including p53, signaling their destruction by the 26S proteasome to keep cellular p53 levels low.
“Mdm2 typically functions as an E3 ubiquitin ligase and conjugates ubiquitin to several proteins including, the tumor suppressor p53. This ultimately signals for destruction by the 26S proteasome to keep cellular p53 levels low [1,2].”
From Integration of DNA damage and repair with murine double-minute 2 (Mdm2) in tumorigenesis (2012) · cites this paper as [1]

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Plant RanGAPs are localized at the nuclear envelope in interphase and associated with microtubules in mitotic cells
Páy, A., Resch, K., Frohnmeyer, H., Fejes, E., Nagy, F., & Nick, P. (2002) · The Plant Journal · doi:10.1046/j.1365-313x.2002.01324.x · Cited by 124 · see citing works
Inhibition of p53 degradation by Mdm2 acetylation
Wang, X., Taplick, J., Geva, N., & Oren, M. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00168-1 · Cited by 108 · see citing works
MSL2 Promotes Mdm2-independent Cytoplasmic Localization of p53
Kruse, J.-P., & Gu, W. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805658200 · Cited by 99 · see citing works
Self-citation
Mdm2 and Mdm4 Loss Regulates Distinct p53 Activities
Barboza, J., Iwakuma, T., Terzian, T., El‐Naggar, A. K., & Lozano, G. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-2079 · Cited by 89 · see citing works
CARPs Are Ubiquitin Ligases That Promote MDM2-independent p53 and Phospho-p53ser20 Degradation
Yang, W., Rozan, L. M., McDonald, E. R., Navaraj, A., Liu, J. J., Matthew, E. M., Wang, W., Dicker, D. T., & El‐Deiry, W. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610793200 · Cited by 88 · see citing works
A phase I trial of intravenous infusion of ONYX-015 and enbrel in solid tumor patients
Nemunaitis, J. J., Senzer, N. N., Sarmiento, S., Zhang, Y.-A., Arzaga, R., Sands, B. E., Maples, P. B., & Tong, A. W. (2007) · Cancer Gene Therapy · doi:10.1038/sj.cgt.7701080 · Cited by 86 · see citing works
Regulation of p53 family members by the ubiquitin-like SUMO system
Stehmeier, P., & Muller, S. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.002 · Cited by 83 · see citing works
Roles of HAUSP-mediated p53 regulation in central nervous system development
Kon, N., Zhong, J., Kobayashi, Y., Li, M., Szabolcs, M., Ludwig, T., Canoll, P. D., & Gu, W. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.12 · Cited by 79 · see citing works
Self-citation
The Role of Ubiquitination in the Direct Mitochondrial Death Program of p53
Marchenko, N. D., & Moll, U. M. (2007) · Cell Cycle · doi:10.4161/cc.6.14.4503 · Cited by 73 · see citing works
Ubiquitination of p53 at Multiple Sites in the DNA-Binding Domain
Chan, W. M., Mak, M. C., Fung, T. K., Lau, A. W. S., Siu, W. Y., & Poon, R. Y. C. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0097 · Cited by 70 · see citing works
NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways
Liu, G., & Xirodimas, D. P. (2010) · Oncogene · doi:10.1038/onc.2009.494 · Cited by 65 · see citing works
Crippling p53 activities via knock-in mutations in mouse models
Iwakuma, T., & Lozano, G. (2007) · Oncogene · doi:10.1038/sj.onc.1210278 · Cited by 63 · see citing works
A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model.
Becker, K., Marchenko, N., Palacios, G., & Moll, U. M. (2008) · Cell Cycle · doi:10.4161/cc.7.9.5756 · Cited by 63 · see citing works
A new map to understand deubiquitination
Katz, E. J., Isasa, M., & Crosas, B. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380021 · Cited by 53 · see citing works
Excess HDM2 Impacts Cell Cycle and Apoptosis and Has a Selective Effect on p53-dependent Transcription
Ohkubo, S., Tanaka, T., Taya, Y., Kitazato, K., & Prives, C. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601388200 · Cited by 47 · see citing works
Mouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo
Wahl, G. M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401911 · Cited by 37 · see citing works
Targeted genetic and viral therapy for advanced head and neck cancers
Huang, P., Chang, J.-F., Kirn, D. H., & Liu, T. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2009.03.008 · Cited by 27 · see citing works

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The hallmarks of cancer
Gutschner, T., & Diederichs, S. (2012) · RNA Biology · doi:10.4161/rna.20481 · Cited by 1,803 · see citing works
MEG3 noncoding RNA: a tumor suppressor
Zhou, Y., Zhang, X., & Klibanski, A. (2012) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0008 · Cited by 717 · see citing works
Regulation of DNA Damage Responses by Ubiquitin and SUMO
Jackson, S. P., & Durocher, D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.017 · Cited by 601 · see citing works
Short Linear Motifs: Ubiquitous and Functionally Diverse Protein Interaction Modules Directing Cell Regulation
Roey, K. V., Uyar, B., Weatheritt, R. J., Dinkel, H., Seiler, M., Budd, A., Gibson, T. J., & Davey, N. E. (2014) · Chemical Reviews · doi:10.1021/cr400585q · Cited by 496 · see citing works
Oncogenic lncRNA downregulates cancer cell antigen presentation and intrinsic tumor suppression
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Clinical Overview of MDM2/X-Targeted Therapies
Burgess, A., Chia, K. M., Haupt, S., Thomas, D., Haupt, Y., & Lim, E. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00007 · Cited by 315 · see citing works
The Roles of MDM2 and MDMX in Cancer
Karni-Schmidt, O., Lokshin, M., & Prives, C. L. (2016) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040349 · Cited by 294 · see citing works
Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects
Scheffner, M., & Kumar, S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.024 · Cited by 285 · see citing works
Inhibition of pluripotent stem cell-derived teratoma formation by small molecules
Lee, M.-O., Moon, S. H., Jeong, H.-C., Yi, J.-Y., Lee, T.-H., Shim, S. H., Rhee, Y.-H., Lee, S.-H., Oh, S.-J., Lee, M.-Y., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303669110 · Cited by 246 · see citing works
Iron Metabolism Regulates p53 Signaling through Direct Heme-p53 Interaction and Modulation of p53 Localization, Stability, and Function
Shen, J., Sheng, X., Chang, Z., Wu, Q., Wang, S., Xuan, Z., Li, D., Wu, Y., Shang, Y., Kong, X., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.042 · Cited by 215 · see citing works
Role of Ubiquitin Ligases and the Proteasome in Oncogenesis: Novel Targets for Anticancer Therapies
Micel, L. N., Tentler, J. J., Smith, P. G., & Eckhardt, G. S. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.44.0958 · Cited by 176 · see citing works
Limiting the power of p53 through the ubiquitin proteasome pathwayPreprint
Pant, V., & Lozano, G. (2014) · Genes & Development · doi:10.1101/gad.247452.114 · Cited by 165 · see citing works
The role of ubiquitin-specific peptidases in cancer progression
Young, M.-J., Hsu, K., Lin, T. E., Chang, W., & Hung, J. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0522-0 · Cited by 161 · see citing works
Reactive Oxygen Species Induced p53 Activation: DNA Damage, Redox Signaling, or Both?
Shi, T., & Dansen, T. B. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8074 · Cited by 164 · see citing works
Mechanisms of p53 degradation
Chao, C. C. ‐. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.08.015 · Cited by 152 · see citing works
Parkinson's disease and cancer: two wars, one front
Devine, M. J., Plun‐Favreau, H., & Wood, N. W. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3150 · Cited by 153 · see citing works
Ferredoxin reductase is critical for p53-dependent tumor suppression via iron regulatory protein 2Preprint
Zhang, Y., Qian, Y., Zhang, J., Yan, W., Jung, Y.-S., Chen, M., Huang, E. C., Lloyd, K. C. K., Duan, Y., Wang, J., et al. (2017) · Genes & Development · doi:10.1101/gad.299388.117 · Cited by 151 · see citing works
NADPH oxidases: key modulators in aging and age-related cardiovascular diseases?
Sahoo, S., Meijles, D. N., & Pagano, P. J. (2016) · Clinical Science · doi:10.1042/cs20150087 · Cited by 146 · see citing works
APCCdc20 Suppresses Apoptosis through Targeting Bim for Ubiquitination and Destruction
Wan, L., Tan, M., Yang, J., Inuzuka, H., Dai, X., Wu, T., Liu, J., Shaik, S., Chen, G., Deng, J., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.04.022 · Cited by 136 · see citing works
Nucleotide Biosynthetic Enzyme GMP Synthase Is a TRIM21-Controlled Relay of p53 Stabilization
Reddy, B. A., van der Knaap, J. A., Bot, A. G. M., Mohd-Sarip, A., Dekkers, D. H. W., Timmermans, M. A. M., Martens, J. W. M., Demmers, J., & Verrijzer, C. P. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.017 · Cited by 131 · see citing works
The Deubiquitylating Enzyme USP44 Counteracts the DNA Double-strand Break Response Mediated by the RNF8 and RNF168 Ubiquitin Ligases
Mosbech, A., Lukas, C., Bekker‐Jensen, S., & Mailand, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.459917 · Cited by 131 · see citing works
Activation and control of p53 tetramerization in individual living cells
Gaglia, G., Guan, Y., Shah, J. V., & Lahav, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311126110 · Cited by 126 · see citing works
p53 N-terminal phosphorylation: a defining layer of complex regulation
Jenkins, L. M. M., Durell, S. R., Mazur, S. J., & Appella, E. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs145 · Cited by 119 · see citing works
SCFFbxo22-KDM4A targets methylated p53 for degradation and regulates senescence
Johmura, Y., Sun, J. M., Kitagawa, K., Nakanishi, K., Kuno, T., Naiki‐Ito, A., Sawada, Y., Miyamoto, T., Okabe, A., Aburatani, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms10574 · Cited by 119 · see citing works
TSLP Induces Mast Cell Development and Aggravates Allergic Reactions through the Activation of MDM2 and STAT6
Han, N., Oh, H., Nam, S., Moon, P., Do‐Won, K. I. M., Kim, H.-M., & Jeong, H. (2014) · Journal of Investigative Dermatology · doi:10.1038/jid.2014.198 · Cited by 118 · see citing works
Dynamic Methylation of Numb by Set8 Regulates Its Binding to p53 and Apoptosis
Dhami, G. K., Liu, H., Galka, M., Voss, C., Wei, R., Muranko, K., Kaneko, T., Cregan, S. P., Li, L., & Li, S. S. ‐. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.028 · Cited by 117 · see citing works
Potential applications of MEG3 in cancer diagnosis and prognosis
He, Y., Luo, Y., Liang, B., Ye, L., Lu, G., & He, W. (2017) · Oncotarget · doi:10.18632/oncotarget.19931 · Cited by 117 · see citing works
Regulators of Oncogenic Mutant TP53 Gain of Function
Yamamoto, S., & Iwakuma, T. (2018) · Cancers · doi:10.3390/cancers11010004 · Cited by 111 · see citing works
Mdm2 and MdmX partner to regulate p53
Wang, X., & Jiang, X. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.02.049 · Cited by 111 · see citing works
p53 stability is regulated by diverse deubiquitinating enzymes
Kwon, S., Saindane, M., & Baek, K. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.08.001 · Cited by 110 · see citing works
TRIM21 – A potential novel therapeutic target in cancer
Alomari, M. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105443 · Cited by 110 · see citing works
A Nuclear Phosphoinositide Kinase Complex Regulates P53
Choi, S., Chen, M., Cryns, V. L., & Anderson, R. A. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0297-2 · Cited by 106 · see citing works
Noncanonical regulation of alkylation damage resistance by the OTUD4 deubiquitinase
Zhao, Y. J., Majid, M. C., Soll, J. M., Brickner, J. R., Dango, S., & Mosammaparast, N. (2015) · The EMBO Journal · doi:10.15252/embj.201490497 · Cited by 97 · see citing works
p53 is activated in response to disruption of the pre-mRNA splicing machinery
Allende-Vega, N., Dayal, S., Agarwala, U., Sparks, A., Bourdon, J., & Saville, M. K. (2012) · Oncogene · doi:10.1038/onc.2012.38 · Cited by 96 · see citing works
cGMP via PKG activates 26S proteasomes and enhances degradation of proteins, including ones that cause neurodegenerative diseases
VerPlank, J. J. S., Tyrkalska, S. D., Fleming, A., Rubinsztein, D. C., & Goldberg, A. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003277117 · Cited by 93 · see citing works
Delineating Crosstalk Mechanisms of the Ubiquitin Proteasome System That Regulate Apoptosis
Gupta, I., Singh, K., Varshney, N. K., & Khan, S. M. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00011 · Cited by 86 · see citing works
Dose and Schedule Determine Distinct Molecular Mechanisms Underlying the Efficacy of the p53–MDM2 Inhibitor HDM201
Jeay, S., Ferretti, S., Holzer, P., Fuchs, J., Chapeau, E. A., Wartmann, M., Sterker, D., Romanet, V., Murakami, M., Kerr, G., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-0338 · Cited by 87 · see citing works
Promoter hypermethylation influences the suppressive role of maternally expressed 3, a long non-coding RNA, in the development of epithelial ovarian cancer
Sheng, X., LI, J., Yang, L., Chen, Z., Zhao, Q., Tan, L., Zhou, Y., & LI, J. (2014) · Oncology Reports · doi:10.3892/or.2014.3208 · Cited by 86 · see citing works
The Tail That Wags the Dog: How the Disordered C-Terminal Domain Controls the Transcriptional Activities of the p53 Tumor-Suppressor Protein
Laptenko, O., Tong, D. R., Manfredi, J., & Prives, C. (2016) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2016.08.011 · Cited by 75 · see citing works
Killing by Degradation: Regulation of Apoptosis by the Ubiquitin-Proteasome-System
Abbas, R., & Larisch, S. (2021) · Cells · doi:10.3390/cells10123465 · Cited by 86 · see citing works
FBXW7 Confers Radiation Survival by Targeting p53 for Degradation
Cui, D., Xiong, X., Shu, J., Dai, X.-Q., Sun, Y., & Zhao, Y. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.12.032 · Cited by 81 · see citing works
Convergence of therapy-induced senescence (TIS) and EMT in multistep carcinogenesis: current opinions and emerging perspectives
Faheem, M. M., Seligson, N. D., Ahmad, S. M., Rasool, R. U., Gandhi, S. G., Bhagat, M., & Goswami, A. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-0286-z · Cited by 80 · see citing works
Novel E3 Ubiquitin Ligases That Regulate Histone Protein Levels in the Budding Yeast Saccharomyces cerevisiae
Singh, R. K., Gonzalez, M., Kabbaj, M.-H. M., & Gunjan, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036295 · Cited by 80 · see citing works
Cullin Family Proteins and Tumorigenesis: Genetic Association and Molecular Mechanisms
Chen, Z., Sui, J., Zhang, F., & Zhang, C. (2015) · Journal of Cancer · doi:10.7150/jca.11076 · Cited by 79 · see citing works
Loss of RDM1 enhances hepatocellular carcinoma progression via p53 and Ras/Raf/ERK pathways
Chen, S.-L., Liu, L., Wang, C., Lu, S.-X., Yang, X., He, Y., Zhang, C. Z., & Yun, J. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12593 · Cited by 77 · see citing works
SCF-Mediated Cdh1 Degradation Defines a Negative Feedback System that Coordinates Cell-Cycle Progression
Fukushima, H., Ogura, K., Wan, L., Lu, Y., Li, V. C., Gao, D., Liu, P., Lau, A. W., Wu, T., Kirschner, M. W., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.031 · Cited by 76 · see citing works
WD Repeat Protein WDR48 in Complex with Deubiquitinase USP12 Suppresses Akt-dependent Cell Survival Signaling by Stabilizing PH Domain Leucine-rich Repeat Protein Phosphatase 1 (PHLPP1)
Gangula, N. R., & Maddika, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.503383 · Cited by 74 · see citing works
Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
Sane, S., & Rezvani, K. S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020442 · Cited by 76 · see citing works
DUBbing Cancer: Deubiquitylating Enzymes Involved in Epigenetics, DNA Damage and the Cell Cycle As Therapeutic Targets
Pinto-Fernández, A., & Kessler, B. M. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00133 · Cited by 73 · see citing works
Extensive Post-translational Modification of Active and Inactivated Forms of Endogenous p53
DeHart, C. J., Chahal, J. S., Flint, S. J., & Perlman, D. H. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030254 · Cited by 70 · see citing works
USP15 potentiates NF‐κB activation by differentially stabilizing TAB2 and TAB3
Zhou, Q., Cheng, C., Wei, Y., Yang, J. X., Zhou, W., Song, Q., Ke, M., Yan, W., Zheng, L., Zhang, Y., et al. (2020) · FEBS Journal · doi:10.1111/febs.15202 · Cited by 69 · see citing works
NUMB phosphorylation destabilizes p53 and promotes self‐renewal of tumor‐initiating cells by a NANOG‐dependent mechanism in liver cancer
Siddique, H. R., Feldman, D. E., Chen, C., Punj, V., Tokumitsu, H., & Machida, K. (2015) · Hepatology · doi:10.1002/hep.27987 · Cited by 67 · see citing works
Ubiquitinated Sirtuin 1 (SIRT1) Function Is Modulated during DNA Damage-induced Cell Death and Survival
Peng, L., Yuan, Z., Li, Y., Ling, H., Izumi, V., Fang, B., Fukasawa, K., Koomen, J. M., Chen, J., & Seto, E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.612796 · Cited by 65 · see citing works
Ovarian tumor domain-containing protein 1 deubiquitinates and stabilizes p53
Piao, S., Pei, H. Z., Huang, B., & Baek, S. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.02.011 · Cited by 65 · see citing works
Merlin, a multi‐suppressor from cell membrane to the nucleus
Zhou, L., & Hanemann, C. O. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.016 · Cited by 64 · see citing works
Mahogunin-mediated α-tubulin ubiquitination via noncanonical K6 linkage regulates microtubule stability and mitotic spindle orientation
Srivastava, D., & Chakrabarti, O. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.1 · Cited by 62 · see citing works
Epigenetic regulation by the menin pathway
Feng, Z., Ma, J., & Hua, X. (2017) · Endocrine Related Cancer · doi:10.1530/erc-17-0298 · Cited by 62 · see citing works
The role of the ubiquitin-proteasome pathway in cancer development and treatment
Ding, F.-B. (2014) · Frontiers in bioscience · doi:10.2741/4254 · Cited by 57 · see citing works
Expression and mechanisms of long non-coding RNA genes MEG3 and ANRIL in gallbladder cancer
Liu, B., Shen, E., Liao, M., Hu, Y., Wu, K., Yang, P., Zhou, L., & Chen, W. (2016) · Tumor Biology · doi:10.1007/s13277-016-4863-y · Cited by 56 · see citing works
Human EHMT2/G9a activates p53 through methylation-independent mechanism
Rada, M., Васильева, Е. А., Lezina, L., Marouco, D. M., Antonov, A. V., Macip, S., Melino, G., & Barlev, N. A. (2016) · Oncogene · doi:10.1038/onc.2016.258 · Cited by 55 · see citing works
Generation and Validation of Intracellular Ubiquitin Variant Inhibitors for USP7 and USP10
Zhang, W., Sartori, M. A., Makhnevych, T., Federowicz, K., Dong, X., Liu, L., Nim, S., Dong, A., Yang, J., Li, Y., et al. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.025 · Cited by 56 · see citing works
Role of Deubiquitinases in Human Cancers: Potential Targeted Therapy
Lai, K. P., Chen, J., & Tse, W. K. F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072548 · Cited by 51 · see citing works
Ubiquitylation of p53 by the APC/C inhibitor Trim39
Zhang, L., Huang, N.-J., Chen, C., Tang, W., & Kornbluth, S. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212047110 · Cited by 51 · see citing works
Recent advances on the intervention sites targeting USP7-MDM2-p53 in cancer therapy
Harakandi, C., Nininahazwe, L., Xu, H., Liu, B., He, C., Zheng, Y., & Zhang, H. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105273 · Cited by 52 · see citing works
Temporal coordination of the transcription factor response to H2O2 stress
Jose, E., March-Steinman, W., Wilson, B. A., Shanks, L., Parkinson, C., Alvarado-Cruz, I., Sweasy, J. B., & Paek, A. L. (2024) · Nature Communications · doi:10.1038/s41467-024-47837-w · Cited by 46 · see citing works
Bifunctional HDAC Therapeutics: One Drug to Rule Them All?
Smalley, J. P., Cowley, S. M., & Hodgkinson, J. T. (2020) · Molecules · doi:10.3390/molecules25194394 · Cited by 47 · see citing works
TRIM21–SERPINB5 aids GMPS repression to protect nasopharyngeal carcinoma cells from radiation-induced apoptosis
Zhang, P., Li, X., He, Q., Zhang, L., Song, K., Yang, X., He, Q., Wang, Y., Hong, X., Ma, J., et al. (2020) · Journal of Biomedical Science · doi:10.1186/s12929-020-0625-7 · Cited by 45 · see citing works
Genetic susceptibility to cervical cancer: role of common polymorphisms in apoptosis-related genes
Tan, S. C., & Ankathil, R. (2015) · Tumor Biology · doi:10.1007/s13277-015-3868-2 · Cited by 44 · see citing works
The regulation of radiosensitivity by p53 and its acetylation
Zhang, J., Shen, L., & Sun, L. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.04.015 · Cited by 45 · see citing works
Proteome Stability as a Key Factor of Genome Integrity
Gumeni, S., Evangelakou, Z., Gorgoulis, V. G., & Trougakos, I. P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102036 · Cited by 41 · see citing works
NuMA Is Required for the Selective Induction of p53 Target Genes
Ohata, H., Miyazaki, M., Otomo, R., Matsushima‐Hibiya, Y., Otsubo, C., Nagase, T., Arakawa, H., Yokota, J., Nakagama, H., Taya, Y., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01221-12 · Cited by 42 · see citing works
Involvement of Phosphoinositide 3-Kinase and PTEN Protein in Mechanism of Activation of TRPC6 Protein in Vascular Smooth Muscle Cells
Monet, M., Francoeur, N. J., & Boulay, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.341354 · Cited by 41 · see citing works
HUWE1 and TRIP12 Collaborate in Degradation of Ubiquitin-Fusion Proteins and Misframed Ubiquitin
Poulsen, E. G., Steinhauer, C., Lees, M. J., Lauridsen, A.-M. B., Ellgaard, L., & Hartmann‐Petersen, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050548 · Cited by 40 · see citing works
Pirh2
Halaby, M., Hakem, R., & Hakem, A. (2013) · Cell Cycle · doi:10.4161/cc.25785 · Cited by 39 · see citing works
V-type nerve agents phosphonylate ubiquitin at biologically relevant lysine residues and induce intramolecular cyclization by an isopeptide bond
Schmidt, C., Breyer, F., Blum, M., Thiermann, H., Worek, F., & John, H. (2014) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-014-7706-y · Cited by 37 · see citing works
Post-translational Modifications of the p53 Protein and the Impact in Alzheimer’s Disease: A Review of the Literature
Clark, J., Kayed, R., Abate, G., Uberti, D. L., Kinnon, P., & Piccirella, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.835288 · Cited by 37 · see citing works
Role of deubiquitinases in DNA damage response
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Authors: Brooks, C. L., & Gu, W.
Affiliations: Stemline Therapeutics (United States) (US)
Columbia University (US)
Corresponding author: Brooks, Christopher L.
ORCID: Brooks, Christopher L.
Gu, Wei
Venue: FEBS Letters
Publisher: Wiley
Published: 2011-05-27
Volume: 585
Issue: 18
Pages: 2803-2809
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/j.febslet.2011.05.022
PMC: PMC3172401
OpenAlex: W2079076511
Cited by: 186
References: 96
Citations by year: 2026: 2 · 2025: 6 · 2024: 9 · 2023: 14 · 2022: 8 · 2021: 15 · 2020: 13 · 2019: 12 · 2018: 9 · 2017: 18 · 2016: 14 · 2015: 13 · 2014: 16 · 2013: 18 · 2012: 17
FWCI: 1.54
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (2r01ca085533-16)
National Cancer Institute (R01-CA085533, R01CA131439, P01CA097403, R01CA118561, P01CA080058, R01CA129627)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Keywords: p53, ubiquitination, ubiquitin, deubiquitination, protein degradation, tumor suppressor regulation, ubiquitin-like proteins, protein localization, protein function regulation
MeSH terms: Animals, Humans, Models, Biological, Transcriptional Activation, Tumor Suppressor Protein p53, Active Transport, Cell Nucleus, Ubiquitin, Proteasome Endopeptidase Complex, Proto-Oncogene Proteins c-mdm2, Ubiquitination

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