p53 ubiquitination: Mdm2 and beyond

Brooks, Christopher L.; Gu, Wei

doi:10.1016/j.molcel.2006.01.020

Cited by 924Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysTGF-β signaling in diseases

p53 ubiquitination: Mdm2 and beyond

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Brooks, Christopher L., Gu, Wei·2006·Molecular Cell

DOI 10.1016/j.molcel.2006.01.020PMC PMC3737769

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Abstract

Although early studies have suggested that the oncoprotein Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. The discoveries of MdmX, HAUSP, ARF, COP1, Pirh2, and ARF-BP1 continue to uncover the multiple facets of this pathway. There is no question that Mdm2 plays a pivotal role in downregulating p53 activities in numerous cellular settings. Nevertheless, growing evidence challenges the conventional view that Mdm2 is essential for p53 turnover.

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Mdm2 facilitates polyubiquitylation and proteasome-dependent degradation of p53.
“Consistent with this, Mdm2 facilitates the polyubiquitylation and proteasome-dependent degradation of p53 [11].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [11]
Other E3 ubiquitin ligases regulate p53 stability and/or localization, such as COP1, Pirh2, ARF-BP1, MSL2, and Parc.
“Other E3 ubiquitin ligases have also been shown to regulate p53 stability and/or localization, such as COP1, Pirh2, ARF-BP1, MSL2, and Parc”
From USP10 Regulates p53 Localization and Stability by Deubiquitinating p53 (2010) · cites this paper as Brooks and Gu, 2006

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Authors: Brooks, C. L., & Gu, W.
Affiliations: Columbia University (US)
Corresponding author: Gu, Wei
ORCID: Brooks, Christopher L.
Gu, Wei
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2006-02
Volume: 21
Issue: 3
Pages: 307-315
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2006.01.020
PMC: PMC3737769
OpenAlex: W2074545297
Semantic Scholar: da08f698f537a1c29961e74498049693d3907fd1
Cited by: 924
References: 94
Citations by year: 2026: 26 · 2025: 29 · 2024: 26 · 2023: 29 · 2022: 34 · 2021: 40 · 2020: 28 · 2019: 38 · 2018: 39 · 2017: 36 · 2016: 44 · 2015: 28 · 2014: 48 · 2013: 39 · 2012: 45
FWCI: 8.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2759 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: Leukemia and Lymphoma Society
University of Texas Southwestern Medical Center
National Institutes of Health (2r01ca085533-16)
National Cancer Institute (R01-CA085533, R01CA131439, P01CA097403, R01CA104843, R01CA098821, R01CA129627)
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 › TGF-β signaling in diseases
Keywords: p53, ubiquitination, MDM2, E3 ubiquitin ligase, p53 degradation, MDMX, USP7, ARF, COP1, Pirh2, tumor suppressor regulation
MeSH terms: Animals, Cell Line, Cell Survival, Humans, Tumor Suppressor Protein p53, Evolution, Molecular, Ubiquitin, Ubiquitin-Protein Ligases, Proto-Oncogene Proteins c-mdm2

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p53 ubiquitination: Mdm2 and beyond

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