Cited by 122Cancer-related Molecular Pathways14-3-3 protein interactionsDNA Repair Mechanisms

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Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3

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LeBron, Cynthia, Chen, Lihong, Gilkes, Daniele M, Chen, Jiandong·2006·The EMBO Journal

DOI 10.1038/sj.emboj.7601032PMC PMC1422166

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Abstract

The MDM2 homolog MDMX is an important regulator of p53 during mouse embryonic development. DNA damage promotes MDMX phosphorylation, nuclear translocation, and degradation by MDM2. Here we show that MDMX copurifies with 14-3-3, and DNA damage stimulates MDMX binding to 14-3-3. Chk2-mediated phosphorylation of MDMX on S367 is important for stimulating 14-3-3 binding, MDMX nuclear import by a cryptic nuclear import signal, and degradation by MDM2. Mutation of MDMX S367 inhibits ubiquitination and degradation by MDM2, and prevents MDMX nuclear import. Expression of 14-3-3 stimulates the degradation of phosphorylated MDMX. Chk2 and 14-3-3 cooperatively stimulate MDMX ubiquitination and overcome the inhibition of p53 by MDMX. These results suggest that MDMX-14-3-3 interaction plays a role in p53 response to DNA damage by regulating MDMX localization and stability.

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Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein
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Ribosomal Protein L11 Negatively Regulates Oncoprotein MDM2 and Mediates a p53-Dependent Ribosomal-Stress Checkpoint Pathway
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Nuclear Export Is Required for Degradation of Endogenous p53 by MDM2 and Human Papillomavirus E6
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Wild-type p53 binds to the TATA-binding protein and represses transcription.
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14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins
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Ribosomal Protein L23 Activates p53 by Inhibiting MDM2 Function in Response to Ribosomal Perturbation but Not to Translation Inhibition
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A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
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ATM associates with and phosphorylates p53: mapping the region of interaction
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High frequency of hypermethylation at the 14-3-3 σ locus leads to gene silencing in breast cancer
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INK4a/ARF: A multifunctional tumor suppressor locus
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“Hereditary human cancers commonly contain alterations to both p16 and ARF (Sharpless 2005).”
Background
Chk2‐deficient mice exhibit radioresistance and defective p53‐mediated transcription
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The 14-3-3 cancer connection
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Phosphorylation of p53 Serine 15 Increases Interaction with CBP
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Chk2 Is a Tumor Suppressor That Regulates Apoptosis in both an Ataxia Telangiectasia Mutated (ATM)-Dependent and an ATM-Independent Manner
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Chk2 kinase — a busy messenger
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Threonine 68 phosphorylation by ataxia telangiectasia mutated is required for efficient activation of Chk2 in response to ionizing radiation.
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Crystal Structure of the 14-3-3ζ:Serotonin N-Acetyltransferase Complex
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Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation
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The Human Myt1 Kinase Preferentially Phosphorylates Cdc2 on Threonine 14 and Localizes to the Endoplasmic Reticulum and Golgi Complex
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Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
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Functional inactivation but not structural mutation of p53 causes liver cancer
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HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53
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Pidd, a new death-domain–containing protein, is induced by p53 and promotes apoptosis
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Inhibition of HDM2 and Activation of p53 by Ribosomal Protein L23
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Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line
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Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
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Intracellular localization of proteasomes
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14-3-3 Interacts Directly with and Negatively Regulates Pro-apoptotic Bax
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STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3
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Mutations in Human ARF Exon 2 Disrupt Its Nucleolar Localization and Impair Its Ability to Block Nuclear Export of MDM2 and p53
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14-3-3ζ Binds a Phosphorylated Raf Peptide and an Unphosphorylated Peptide via Its Conserved Amphipathic Groove
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Hypoxia Links ATR and p53 through Replication Arrest
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The p53 response to DNA damage
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Regulation of mdm2 expression by p53: alternative promoters produce transcripts with nonidentical translation potential.
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Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
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MDM2 interacts with MDMX through their RING finger domains
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Involvement of 14‐3‐3 proteins in nuclear localization of telomerase
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The Ribosomal L5 Protein Is Associated with mdm-2 and mdm-2-p53 Complexes
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Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development
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The mdm-2 oncogene can overcome wild-type p53 suppression of transformed cell growth.
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Amplification of Mdmx (or Mdm4 ) Directly Contributes to Tumor Formation by Inhibiting p53 Tumor Suppressor Activity
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Pharmacologic activation of p53 elicits Bax-dependent apoptosis in the absence of transcription
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14-3-3 proteins; bringing new definitions to scaffolding
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Database of p53 gene somatic mutations in human tumors and cell lines: updated compilation and future prospects
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Nucleophosmin (B23) Targets ARF to Nucleoli and Inhibits Its Function
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The human MDM-2 oncogene is overexpressed in leukemias
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Stabilization of the MDM2 Oncoprotein by Interaction with the Structurally Related MDMX Protein
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Isoforms of 14‐3‐3 protein can form homo‐ and heterodimers in vivo and in vitro: implications for function as adapter proteins
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Repression of p53-mediated transcription by MDM2: a dual mechanism
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Small-Molecule Antagonists of p53-MDM2 Binding: Research Tools and Potential Therapeutics
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Mutual Dependence of MDM2 and MDMX in Their Functional Inactivation of p53
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Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.
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ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage
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Self-citation
Regulation of apoptosis: the ubiquitous way
Yang, Y., & Xiao-dan, Y. (2003) · The FASEB Journal · doi:10.1096/fj.02-0654rev · Cited by 254
Effects of genetic background on tumorigenesis in p53‐deficient mice
Donehower, L. A., Harvey, M., Vogel, H., McArthur, M. J., Montgomery, C. A., Park, S. H., Thompson, T., Ford, R. J., & Bradley, A. (1995) · Molecular Carcinogenesis · doi:10.1002/mc.2940140105 · Cited by 252
14-3-3 Proteins—a focus on cancer and human disease
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An ATR- and Chk1-Dependent S Checkpoint Inhibits Replicon Initiation following UVC-Induced DNA Damage
Heffernan, T. P., Simpson, D. A., Frank, A. R., Heinloth, A. N., Paules, R. S., Cordeiro-Stone, M., & Kaufmann, W. K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8552-8561.2002 · Cited by 251
Essential role of ribosomal protein L11 in mediating growth inhibition‐induced p53 activation
Bhat, K., Itahana, K., Jin, A., & Zhang, Y. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600247 · Cited by 249
MDM2 promotes ubiquitination and degradation of MDMX
Pan, Y., & Chen, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5113-5121.2003 · Cited by 246 · cited 3×
“translocation and degradation by the proteasomes (Li et al, 2002; Pan and Chen, 2003).”
Background
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p53 in recombination and repair
Gatz, S. A., & Wiesmüller, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401903 · Cited by 242
MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin
Hu, B., Gilkes, D. M., Farooqi, B., Sebti, S. M., & Chen, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600147200 · Cited by 236
Targeted expression of MDM2 uncouples S phase from mitosis and inhibits mammary gland development independent of p53.
Lundgren, K., Montes de Oca Luna, R., McNeill, Y. B., Emerick, E. P., Spencer, B., Barfield, C. R., Lozano, G., Rosenberg, M. P., & Finlay, C. A. (1997) · Genes & Development · doi:10.1101/gad.11.6.714 · Cited by 235
Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms
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14-3-3σ Positively Regulates p53 and Suppresses Tumor Growth
Yang, H.-Y., Wen, Y.-Y., Chen, C.-H., Lozano, G., & Lee, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7096-7107.2003 · Cited by 229
Regulation of p53 localization
Liang, S., & Clarke, M. F. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02227.x · Cited by 224
14-3-3 proteins as potential oncogenes
Tzivion, G., Gupta, V. S., Kaplun, L., & Balan, V. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.03.004 · Cited by 222
Tissue and cell-specific expression of the p53-target genes: bax, fas, mdm2 and waf1/p21, before and following ionising irradiation in mice
Bouvard, V., Zaitchouk, T., Vacher, M., Duthu, A., Canivet, M., Choisy, C., Nieruchalski, M., & May, E. (2000) · Oncogene · doi:10.1038/sj.onc.1203366 · Cited by 221
MdmX Protects p53 from Mdm2-Mediated Degradation
Jackson, M. W., & Berberich, S. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1001-1007.2000 · Cited by 211 · cited 5×
“conservation of the p53-binding domain, MDMX was found to bind the N-terminus of p53 and inhibit its transactivation (Jackson and Berberich 2000; Stad, Little et al. 2001).”
BackgroundInfluential
Tumor suppression and normal aging in mice with constitutively high p53 activity
Mendrysa, S. M., O'Leary, K. A., McElwee, M. K., Michalowski, J., Eisenman, R. N., Powell, D. A., & Perry, M. E. (2006) · Genes & Development · doi:10.1101/gad.1378506 · Cited by 210
Multiple Lysine Mutations in the C-Terminal Domain of p53 Interfere with MDM2-Dependent Protein Degradation and Ubiquitination
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
14-3-3 (ϵ) Interacts with the Insulin-like Growth Factor I Receptor and Insulin Receptor Substrate I in a Phosphoserine-dependent Manner
Craparo, A., Freund, R., & Gustafson, T. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11663 · Cited by 196
MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins
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mdmx is a negative regulator of p53 activity in vivo.
Finch, R. A., Donoviel, D. B., Potter, D., Shi, M., Fan, A., Freed, D. D., Wang, C.-Y., Zambrowicz, B., Ramírez‐Solis, R., Sands, A., et al. (2002) · PubMed · Cited by 192
HAUSP is Required for p53 Destabilization
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Comparative study of the p53-mdm2 and p53-MDMX interfaces
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Identification of a cryptic nucleolar-localization signal in MDM2
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Identification of novel mdm2 binding peptides by phage display.
Böttger, V., Böttger, A., Howard, S. F., Picksley, S. M., Chêne, P., Garcı́a-Echeverrı́a, C., Hochkeppel, H. K., & Lane, D. P. (1996) · PubMed · Cited by 182
Phosphorylation of Hdmx mediates its Hdm2- and ATM-dependent degradation in response to DNA damage
Pereg, Y., Shkedy, D., de Graaf, P., Meulmeester, E., Edelson-Averbukh, M., Salek, M., Biton, S., Teunisse, A. F. A. S., Lehmann, W. D., Jochemsen, A. G., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408595102 · Cited by 181
Inhibition of MDM2 by hsp90 Contributes to Mutant p53 Stabilization
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Control of p53 ubiquitination and nuclear export by MDM2 and ARF.
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p53 Activation by Small Molecules: Application in Oncology
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Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: a statistical analysis of information in the National Cancer Institute database
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ATM-Mediated Phosphorylations Inhibit Mdmx/Mdm2 Stabilization by HAUSP in Favor of p53 Activation
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The SV40 a gene product is required for the production of a 54,000 MW cellular tumor antigen
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The role of RB in cell cycle control
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“Several reports showed that MDMX can be ubiquitinated and degraded by MDM2 (de Graaf et al, 2003; Kawai et al, 2003; Pan and Chen, 2003).”
Background
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“Several reports showed that MDMX can be ubiquitinated and degraded by MDM2 (de Graaf et al, 2003; Kawai et al, 2003; Pan and Chen, 2003).”
Background
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Authors: LeBron, C., Chen, L., Gilkes, D. M., & Chen, J.
Affiliations: Moffitt Cancer Center (US)
Corresponding author: Chen, Jiandong
ORCID: Chen, Lihong
Gilkes, Daniele M
Chen, Jiandong
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2006-03-02
Volume: 25
Issue: 6
Pages: 1196-1206
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7601032
PMC: PMC1422166
OpenAlex: W2068624303
Cited by: 122
References: 255
Citations by year: 2025: 2 · 2024: 3 · 2022: 1 · 2021: 6 · 2020: 4 · 2019: 5 · 2018: 2 · 2017: 3 · 2016: 8 · 2015: 2 · 2014: 7 · 2013: 11 · 2012: 9
FWCI: 6.78
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
Funders: American Cancer Society
National Institutes of Health
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Keywords: MDMX, Chk2, MDM2, p53, DNA damage response, nuclear import, protein degradation, ubiquitination, phosphorylation, nuclear import signal, protein stability, mouse embryo development
MeSH terms: Animals, Breast Neoplasms, DNA Damage, Gene Expression Regulation, HeLa Cells, Humans, Nuclear Proteins, Phosphorylation, Protein Binding, Proto-Oncogene Proteins, Osteosarcoma, Tumor Suppressor Protein p53, Mice, Knockout, Cell Cycle Proteins, Active Transport, Cell Nucleus, Ubiquitin, Immunoprecipitation, 14-3-3 Proteins, Cyclin-Dependent Kinase 2, Mice

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Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3

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