Cited by 724Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysHeat shock proteins research

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Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53

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Honda, Reiko, Yasuda, Hideyo·1999·The EMBO Journal

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Abstract

We have demonstrated previously that the oncoprotein Mdm2 has a ubiquitin ligase activity for the tumor suppressor p53 protein. In the present study, we characterize this ubiquitin ligase activity of Mdm2. We first demonstrate the ubiquitination of several p53 point mutants and deletion mutants by Mdm2. The point mutants, which cannot bind to Mdm2, are not ubiquitinated by Mdm2. The ubiquitination of the C-terminal deletion mutants, which contain so-called Mdm2-binding sites, is markedly decreased, compared with that of wild-type p53. The binding of Mdm2 to p53 is essential for ubiquitination, but p53's tertiary structure and/or C-terminal region may also be important for this reaction. DNA-dependent protein kinase is known to phosphorylate p53 on Mdm2-binding sites, where DNA damage induces phosphorylation, and p53 phosphorylated by this kinase is not a good substrate for Mdm2. This suggests that DNA damage-induced phosphorylation stabilizes p53 by inhibiting its ubiquitination by Mdm2. We further investigated whether the tumor suppressor p19(ARF) affects the ubiquitin ligase activity of Mdm2 for p53. The activity of p19(ARF)-bound Mdm2 was found to be lower than that of free Mdm2, suggesting that p19(ARF) promotes the stabilization of p53 by inactivating Mdm2.

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Background
A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia
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Authors: Honda, R., & Yasuda, H.
Affiliations: Tokyo University of Pharmacy and Life Sciences (JP)
Corresponding author: Yasuda, Hideyo
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1999-01-04
Volume: 18
Issue: 1
Pages: 22-27
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/18.1.22
PMC: PMC1171098
OpenAlex: W2028210102
Cited by: 724
References: 43
Citations by year: 2026: 1 · 2025: 3 · 2024: 3 · 2023: 12 · 2022: 12 · 2021: 3 · 2020: 10 · 2019: 4 · 2018: 11 · 2017: 5 · 2016: 14 · 2015: 19 · 2014: 20 · 2013: 24 · 2012: 20
FWCI: 33.88
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: European Molecular Biology Organization
Institute of Genetics
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: p19ARF, MDM2, p53, ubiquitin ligase activity, p53 ubiquitination, p53 stabilization, DNA-dependent protein kinase, p53 phosphorylation, DNA damage response, tumor suppressor proteins, protein-protein interaction
MeSH terms: Animals, Cell Line, Cloning, Molecular, DNA-Binding Proteins, HeLa Cells, Humans, Ligases, Mutation, Nuclear Proteins, Phosphorylation, Proteins, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Ubiquitins, Tumor Suppressor Protein p53, Protein Serine-Threonine Kinases, Spodoptera, Tumor Suppressor Protein p14ARF, Ubiquitin-Protein Ligases, Proto-Oncogene Proteins c-mdm2, DNA-Activated Protein Kinase, In Vitro Techniques

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Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53

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