Cited by 169Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysHeat shock proteins research

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Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo

Xirodimas, Dimitris, Saville, Mark K, Edling, Charlotte, Lane, David P, Laín, Sonia·2001·Oncogene

DOI 10.1038/sj.onc.1204656

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Abstract

Mdm2 has been shown to promote its own ubiquitination and the ubiquitination of the p53 tumour suppressor by virtue of its E3 ubiquitin ligase activity. This modification targets Mdm2 and p53 for degradation by the proteasome. The p14ARF tumour suppressor has been shown to inhibit degradation of p53 mediated by Mdm2. Several models have been proposed to explain this effect of p14ARF. Here we have compared the effects of p14ARF overexpression on the in vivo ubiquitination of p53 and Mdm2. We report that the inhibition of the Mdm2-mediated degradation of p53 by p14ARF is associated with a decrease in the proportion of ubiquitinated p53. The levels of polyubiquitinated p53 decreased preferentially compared to monoubiquitinated species. p14ARF overexpression increased the levels of Mdm2 but it did not reduce the overall levels of ubiquitinated Mdm2 in vivo. This is unexpected because p14ARF has been reported to inhibit the ubiquitination of Mdm2 in vitro. In addition we show that like p14ARF, the proteasome inhibitor MG132 can promote the accumulation of Mdm2 in the nucleolus and that this can occur in the absence of p14ARF expression. We also show that the mutation of the nucleolar localization signal of Mdm2 does not impair the overall ubiquitination of Mdm2 but is necessary for the effective polyubiquitination of p53. These studies reveal important differences in the regulation of the stability of p53 and of Mdm2.

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Authors: Xirodimas, D., Saville, M. K., Edling, C., Lane, D. P., & Laín, S.
Affiliations: University of Dundee (GB)
ORCID: Xirodimas, Dimitris
Saville, Mark K
Edling, Charlotte
Lane, David P
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2001-08-16
Volume: 20
Issue: 36
Pages: 4972-4983
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1204656
OpenAlex: W2050259175
Cited by: 169
References: 37
Citations by year: 2024: 2 · 2023: 1 · 2021: 4 · 2020: 2 · 2019: 6 · 2018: 6 · 2017: 5 · 2016: 3 · 2015: 5 · 2014: 6 · 2013: 6 · 2012: 9
FWCI: 5.55
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (publishedVersion)
HAL (submittedVersion)
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: p14ARF, p53, MDM2, ubiquitination, polyubiquitination, monoubiquitination, proteasomal degradation, E3 ubiquitin ligase, protein stability, nucleolar localization signal, MG132, tumor suppressor regulation
MeSH terms: Animals, Cell Line, Cell Nucleolus, Cysteine Endopeptidases, Leupeptins, Multienzyme Complexes, Nuclear Proteins, Proteins, Proto-Oncogene Proteins, Transfection, Ubiquitins, Cysteine Proteinase Inhibitors, Tumor Suppressor Protein p53, Tumor Suppressor Protein p14ARF, Proteasome Endopeptidase Complex, Proto-Oncogene Proteins c-mdm2

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Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo

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