Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity
Open accessAbstract
The only reported role for the conjugation of the NEDD8 ubiquitin-like molecule is control of the activity of SCF ubiquitin ligase complexes. Here, we show that the Mdm2 RING finger E3 ubiquitin ligase can also promote NEDD8 modification of the p53 tumor suppressor protein. Mdm2 is itself modified with NEDD8 with very similar characteristics to the autoubiquitination activity of Mdm2. By using a cell line (TS-41) with a temperature-sensitive mutation in the NEDD8 conjugation pathway and a p53 mutant that cannot be NEDDylated (3NKR), we demonstrate that Mdm2-dependent NEDD8 modification of p53 inhibits its transcriptional activity. These findings expand the role for Mdm2 as an E3 ligase, providing evidence that Mdm2 is a common component of the ubiquitin and NEDD8 conjugation pathway and indicating the diverse mechanisms by which E3 ligases can control the function of substrate proteins.
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Mdm2 promotes conjugation of NEDD8 to itself and to p53.
“Mdm2 also promotes the conjugation of NEDD8 (another Ubl molecule), to itself and to p53 [124].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [124]
Replacing these lysines with arginine leads to increased p53 transcriptional activity in vitro, suggesting that NEDDylation of p53 inhibits its function.
“Replacing these lysines with arginine leads to increased p53 transcriptional activity in vitro, suggesting that NEDDylation of p53 inhibits its function.”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [124]
Mdm2-mediated NEDDylation occurs at a restricted subset of p53 lysines: K370, K372, and K373.
“Although Mdm2 ubiquitylates several C-terminal lysines of p53, Mdm2-mediated NEDDylation occurs at a restricted subset of them (K370, K372, K373).”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [124]
Cites
Phosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766 · see citing works
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · see citing works
Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951 · see citing works
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,472 · see citing works
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420 · cited 2× · see citing works
“Cysteine 462 (464 in human) has been pretion of the p53 gene (Jones et al., 1995; Luna et al., 1995).”
BackgroundThe ubiquitin–proteasome pathway: on protein death and cell life
Ciechanover, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7151 · Cited by 1,419 · see citing works
Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · cited 2× · see citing works
“Cysteine 462 (464 in human) has been pretion of the p53 gene (Jones et al., 1995; Luna et al., 1995).”
BackgroundSCF and Cullin/RING H2-Based Ubiquitin Ligases
Deshaies, R. J. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.435 · Cited by 1,238 · see citing works
Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53
Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044 · see citing works
Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,027 · see citing works
The p53–Mdm2 module and the ubiquitin system
Michael, D., & Oren, M. (2002) · Seminars in Cancer Biology · doi:10.1016/s1044-579x(02)00099-8 · Cited by 759 · see citing works
Mapping of the p53 and mdm-2 Interaction Domains
Chen, J., Maréchal, V., & Levine, A. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.7.4107 · Cited by 689 · see citing works
SUMO‐1 modification activates the transcriptional response of p53
Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Midgley, C., Lane, D. P., & Hay, R. T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6455 · Cited by 639 · see citing works
Self-citationEverett, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., & Parkinson, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1519 · Cited by 491 · see citing works
Querido, E., Blanchette, P., Yan, Q., Kamura, T., Morrison, M. R., Boivin, D., Kaelin, W. G., Conaway, R. C., Conaway, J. W., & Branton, P. E. (2001) · Genes & Development · doi:10.1101/gad.926401 · Cited by 480 · see citing works
COP9 signalosome‐specific phosphorylation targets p53 to degradation by the ubiquitin system
Bech‐Otschir, D., Kraft, R., Huang, X., Henklein, P., Kapelari, B., Pollmann, C., & Dubiel, W. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1630 · Cited by 396 · see citing works
Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation
Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Lane, D. P., & Hay, R. T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8458-8467.2000 · Cited by 386 · see citing works
Self-citationHonda, R., & Yasuda, H. (2000) · Oncogene · doi:10.1038/sj.onc.1203464 · Cited by 376 · see citing works
Deregulated degradation of the cdk inhibitor p27 and malignant transformation
Bloom, J., & Pagano, M. (2002) · Seminars in Cancer Biology · doi:10.1016/s1044-579x(02)00098-6 · Cited by 374 · see citing works
Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo
Böttger, A., Böttger, V., Sparks, A., Liu, W.-L., Howard, S. F., & Lane, D. P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00374-5 · Cited by 363 · see citing works
Self-citationA novel protein modification pathway related to the ubiquitin system
Liakopoulos, D., Doenges, G., Matuschewski, K., & Jentsch, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.8.2208 · Cited by 361 · see citing works
NEDD8 recruits E2‐ubiquitin to SCF E3 ligase
Kawakami, T., Chiba, T., Suzuki, T., Iwai, K., Yamanaka, K., Minato, N., Suzuki, H., Shimbara, N., Hidaka, Y., Osaka, F., et al. (2001) · EMBO Journal · doi:10.1093/emboj/20.15.4003 · Cited by 344 · see citing works
Activation of the p53 tumor suppressor protein
Vousden, K. H. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00035-5 · Cited by 337 · see citing works
Proteasome-Mediated Degradation of p21 via N-Terminal Ubiquitinylation
Bloom, J., Amador, V., Bartolini, F., Demartino, G., & Pagano, M. (2003) · Cell · doi:10.1016/s0092-8674(03)00755-4 · Cited by 322 · see citing works
NEDD8 Modification of CUL1 Dissociates p120CAND1, an Inhibitor of CUL1-SKP1 Binding and SCF Ligases
Liu, J., Furukawa, M., Matsumoto, T., & Xiong, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00783-9 · Cited by 319 · see citing works
Coordinate regulation of contractile protein synthesis during myoblast differentiation
Devlin, R. B., & Emerson, C. P. (1978) · Cell · doi:10.1016/0092-8674(78)90211-8 · Cited by 315 · see citing works
Lammer, D., Mathias, N., Laplaza, J. M., Jiang, W., Liu, Y., Callis, J., Goebl, M. G., & Estelle, M. A. (1998) · Genes & Development · doi:10.1101/gad.12.7.914 · Cited by 312 · see citing works
Identification of the Activating and Conjugating Enzymes of the NEDD8 Conjugation Pathway
Gong, L., & Yeh, E. T. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.12036 · Cited by 273 · see citing works
Kamura, T., Conrad, M. N., Yan, Q., Conaway, R. C., & Conaway, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.22.2928 · Cited by 270 · see citing works
A new NEDD8-ligating system for cullin-4APreprint
Osaka, F., Kawasaki, H., Aida, N., Saeki, M., Chiba, T., Kawashima, S., Tanaka, K., & Kato, S. (1998) · Genes & Development · doi:10.1101/gad.12.15.2263 · Cited by 255 · see citing works
Midgley, C., Desterro, J. M. P., Saville, M. K., Howard, S. F., Sparks, A., Hay, R. T., & Lane, D. P. (2000) · Oncogene · doi:10.1038/sj.onc.1203593 · Cited by 250 · see citing works
Self-citationMdmx stabilizes p53 and Mdm2 via two distinct mechanisms
Stad, R., Little, N. A., Xirodimas, D. P., Frenk, R., van der Eb, A. J., Lane, D. P., Saville, M. K., & Jochemsen, A. G. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve227 · Cited by 234 · see citing works
Self-citationMendrysa, S. M., McElwee, M. K., Michalowski, J., O'Leary, K. A., Young, K. M., & Perry, M. E. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.2.462-473.2003 · Cited by 234 · see citing works
The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice
Tateishi, K., Omata, M., Tanaka, K., & Chiba, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104035 · Cited by 230 · see citing works
Covalent modifier NEDD8 is essential for SCF ubiquitin‐ligase in fission yeast
Osaka, F., Saeki, M., Katayama, S., Aida, N., Toh‐e, A., Kominami, K., Toda, T., Suzuki, T., Chiba, T., Tanaka, K., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3475 · Cited by 217 · see citing works
The von Hippel–Lindau Tumor Suppressor Gene
Kondo, K., & Kaelin, W. G. (2001) · Experimental Cell Research · doi:10.1006/excr.2000.5139 · Cited by 215 · see citing works
The Ubiquitin-Related Protein RUB1 and Auxin Response in Arabidopsis
del Pozo, J. C., Timpte, C., Tan, S., Callis, J., & Estelle, M. A. (1998) · Science · doi:10.1126/science.280.5370.1760 · Cited by 215 · see citing works
The von Hippel-Lindau Tumor Suppressor Gene
Elias, R. M., Zhang, Q. H., & Brugarolas, J. (2020) · The Cancer Journal · doi:10.1097/ppo.0000000000000480 · Cited by 209 · see citing works
NEDP1, a Highly Conserved Cysteine Protease That deNEDDylates Cullins
Mendoza, H. M., Shen, L., Botting, C. H., Lewis, A., Chen, J., Ink, B. S., & Hay, R. T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212948200 · Cited by 207 · see citing works
Self-citationCytoskeletal Regulation by the Nedd8 Ubiquitin-Like Protein Modification Pathway
Kurz, T., Pintard, L., Willis, J. H., Hamill, D. R., Gönczy, P., Peter, M., & Bowerman, B. A. (2002) · Science · doi:10.1126/science.1067765 · Cited by 204 · see citing works
Nakamura, S., Roth, J. A., & Mukhopadhyay, T. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9391-9398.2000 · Cited by 198 · see citing works
The ubiquitin‐proteasome pathway
Roos‐Mattjus, P., & Sistonen, L. (2004) · Annals of Medicine · doi:10.1080/07853890310016324 · Cited by 185 · see citing works
Stephen, C. W., Helminen, P., & Lane, D. P. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0202 · Cited by 180 · see citing works
Self-citationAn intact NEDD8 pathway is required for Cullin‐dependent ubiquitylation in mammalian cells
Ohh, M., Kim, W. Y., Moslehi, J. J., Chen, Y., Chau, V., Read, M. A., & Kaelin, W. G. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf028 · Cited by 177 · see citing works
Role of the Arabidopsis RING-H2 Protein RBX1 in RUB Modification and SCF Function
Gray, W. M., Hellmann, H. A., Dharmasiri, S., & Estelle, M. A. (2002) · The Plant Cell · doi:10.1105/tpc.003178 · Cited by 173 · see citing works
Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo
Xirodimas, D., Saville, M. K., Edling, C., Lane, D. P., & Laín, S. (2001) · Oncogene · doi:10.1038/sj.onc.1204656 · Cited by 169 · see citing works
Self-citationLykke‐Hartmann, K., Schaefer, L., Menon, S., Deng, X., Miller, J. B., & Wei, N. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.19.6790-6797.2003 · Cited by 140 · see citing works
Chen, Y., McPhie, D. L., Hirschberg, J., & Neve, R. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8929 · Cited by 137 · see citing works
Cocompartmentalization of p53 and Mdm2 Is a Major Determinant for Mdm2-Mediated Degradation of p53
Xirodimas, D. P., Stephen, C. W., & Lane, D. P. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5314 · Cited by 127 · see citing works
Self-citationYan, J., Walz, K., Nakamura, H., Carattini-Rivera, S., Zhao, Q., Vogel, H. S., Wei, N., Justice, M. J., Bradley, A., & Lupski, J. R. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.19.6798-6808.2003 · Cited by 104 · see citing works
Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E3 ligase and regulates its stability
Morimoto, M., Nishida, T., Nagayama, Y., & Yasuda, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)03051-6 · Cited by 98 · see citing works
P14ARF promotes accumulation of SUMO-1 conjugated (H)Mdm2
Xirodimas, D. P., Chisholm, J., Desterro, J. M. S., Lane, D. P., & Hay, R. T. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03310-0 · Cited by 94 · see citing works
Self-citationHandeli, S., & Weintraub, H. (1992) · Cell · doi:10.1016/0092-8674(92)90594-3 · Cited by 88 · see citing works
The SAR1 gene of Arabidopsis acts downstream of the AXR1 gene in auxin response
Cernac, A., Lincoln, C., Lammer, D., et al. (1997) · Development · doi:10.1242/dev.124.8.1583 · Cited by 84 · see citing works
Wu, K. K.-Y., Chen, A., Tan, P., & Pan, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108008200 · Cited by 82 · see citing works
Liu, W.-L., Midgley, C., Stephen, C. W., Saville, M. K., & Lane, D. P. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5082 · Cited by 38 · see citing works
Self-citationExploiting the p53 pathway for cancer diagnosis and therapy
Woods, Y. L., & Lane, D. P. (2003) · The Hematology Journal · doi:10.1038/sj.thj.6200260 · Cited by 28 · see citing works
Self-citationProtecting p53 from degradation
Laı́n, S. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310482 · Cited by 14 · see citing works
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Self-citationCoping with stress: multiple ways to activate p53
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The p53 orchestra: Mdm2 and Mdmx set the tone
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Liu, Y., Tavana, O., & Gu, W. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz060 · Cited by 392 · see citing works
Mdm2-mediated ubiquitylation: p53 and beyond
Marine, J.-C., & Lozano, G. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.68 · Cited by 354 · see citing works
Keeping p53 in check: essential and synergistic functions of Mdm2 and Mdm4
Marine, J.-C., Francoz, S., Maetens, M., Wahl, G., Toledo, F., & Lozano, G. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401912 · Cited by 352 · see citing works
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The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2
Stevenson, L. F., Sparks, A., Allende‐Vega, N., Xirodimas, D. P., Lane, D. P., & Saville, M. K. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601567 · Cited by 280 · see citing works
Self-citationFeng, L., Lin, T., Uranishi, H., Gu, W., & Xu, Y. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5389-5395.2005 · Cited by 236 · see citing works
Marine, J.-C. W., Dyer, M. A., & Jochemsen, A. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.03362 · Cited by 228 · see citing works
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Regulation of nucleolar signalling to p53 through NEDDylation of L11
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- Authors
- Xirodimas, D. P., Saville, M. K., Bourdon, J.-C., Hay, R. T., & Lane, D. P.
- Affiliations
- University of Dundee (GB)
- University of St Andrews (GB)
- Corresponding author
- Lane, David P
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2004-07
- Volume
- 118
- Issue
- 1
- Pages
- 83-97
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2168979257
- Cited by
- 570
- References
- 59
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- FWCI
- 14.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
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- Locations
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- Discovery Research Portal (University of Dundee) (submittedVersion)
- 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
- MDM2, neddylation, p53, E3 ubiquitin ligase, ring finger, autoubiquitination, transcriptional activity, tumor suppressor regulation, ubiquitin-like modification, SCF ubiquitin ligase
- MeSH terms
- Animals, Cell Line, Chlorocebus aethiops, Cricetulus, DNA Damage, Cricetinae, Humans, Ligases, Lysine, Models, Biological, Mutation, Nuclear Proteins, Proto-Oncogene Proteins, Temperature, Ultraviolet Rays, Transcriptional Activation, Tumor Suppressor Protein p53, CHO Cells, COS Cells, Ubiquitin, Cell Line, Tumor, Mice, Proto-Oncogene Proteins c-mdm2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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