Cited by 178Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysTGF-β signaling in diseases

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Inactivation of HAUSP in vivo modulates p53 function.

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Kon, N, Kobayashi, Y, Li, M, Brooks, C L, Ludwig, T, Gu, W·2010·Oncogene

DOI 10.1038/onc.2009.427PMC PMC2857765

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Abstract

Hausp is a deubiquitinase that has been shown to regulate the p53-Mdm2 pathway. Cotransfection of p53 and Hausp stabilizes p53 through the removal of ubiquitin moieties from polyubiquitinated p53. Interestingly, knockout or RNA interference-mediated knockdown of Hausp in human cells also resulted in the stabilization of p53 due to the destabilization of Mdm2, suggesting a dynamic role of Hausp in p53 activation. To understand the physiological functions of Hausp, we generated hausp knockout mice. Hausp knockout mice die during early embryonic development between embryonic days E6.5 and E7.5. The hausp knockout embryos showed p53 activation, but no apparent increase in apoptosis. Embryonic lethality was caused by a dramatic reduction in proliferation and termination in development, in part due to p53 activation and/or abrogation of p53-independent functions. Although deletion of p53 did not completely rescue the embryonic lethality of the hausp knockout, embryonic development was extended in both hausp and p53 double knockout embryos. These data show that Hausp has a critical role in regulating the p53-Mdm2 pathway.

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Imanci, A. (2023) · theses.fr (ABES) · doi:10.70675/42ed1cefz7195z4db8z9d27zc481ff5a90e7
Proteome-wide Ubiquitinome Profiling Reveals Substrate-specific Dynamics Within the USP7 Network
van der Meer, J. W., van der Knaap, J. A., Sijm, A., Bezstarosti, K., Dekkers, D. H. W., Doff, W. A. S., Demmers, J., & Verrijzer, C. P. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101602
Targeting USP7 in sarcomas: opportunities and challenges
Franzese, S., & Cassinelli, G. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118319
BindingDB Entry 50018466: Recent advances in the development of ubiquitin-specific-processing protease 7 (USP7) inhibitors.
BindingDB (2024) · UC San Diego · doi:10.7270/q2bv7mvn
BindingDB Entry 50001159: Chemical Approaches to Intervening in Ubiquitin Specific Protease 7 (USP7) Function for Oncology and Immune Oncology Therapies.
BindingDB (2020) · UC San Diego · doi:10.7270/q2cr5wvg

Authors: Kon, N., Kobayashi, Y., Li, M., Brooks, C. L., Ludwig, T., & Gu, W.
Affiliations: Columbia University (US)
ORCID: Kon, N
Brooks, C L
Ludwig, T
Gu, W
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2009-11-30
Volume: 29
Issue: 9
Pages: 1270-1279
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/onc.2009.427
PMC: PMC2857765
OpenAlex: W2037667982
Cited by: 176
References: 31
Citations by year: 2026: 2 · 2025: 3 · 2024: 8 · 2023: 7 · 2022: 10 · 2021: 12 · 2020: 28 · 2019: 14 · 2018: 15 · 2017: 15 · 2016: 10 · 2015: 10 · 2014: 8 · 2013: 10 · 2012: 8
FWCI: 3.99
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Cancer Institute (P01CA097403, 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: USP7, p53, MDM2, deubiquitinase, p53 stabilization, MDM2-p53 pathway, embryonic lethality, cell proliferation, knockout mice, p53-independent function, apoptosis
MeSH terms: Ubiquitin-Specific Peptidase 7, Animals, Female, HeLa Cells, Humans, Substrate Specificity, Genes, p53, Tumor Suppressor Protein p53, Apoptosis, Mice, Knockout, Tumor Suppressor Proteins, Ubiquitin, RNA Interference, RNA, Small Interfering, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases, Cell Line, Tumor, Mice, Proto-Oncogene Proteins c-mdm2

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Inactivation of HAUSP in vivo modulates p53 function.

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