Regulation of p53 by the Ubiquitin-conjugating Enzymes UbcH5B/C in Vivo
Open accessAbstract
p53 levels are regulated by ubiquitination and 26 S proteasome-mediated degradation. p53 is a substrate for the E3 ligase Mdm2, however, the ubiquitin-conjugating enzymes (E2s) involved in p53 ubiquitination in intact cells have not been defined previously. To investigate the E2 specificity of Mdm2 we carried out an in vitro screen using a panel of ubiquitin E2s. Of the E2s tested only UbcH5A, -B, and -C and E2-25K support Mdm2-mediated ubiquitination of p53. The same E2s also support Mdm2 auto-ubiquitination. Small interfering RNA-mediated knockdown of UbcH5B/C causes accumulation of Mdm2 and p53 in unstressed cells. We show that suppression of UbcH5B/C inhibits p53 ubiquitination and degradation. Despite up-regulating the level of nuclear p53, UbcH5B/C knockdown does not on its own result in an increase in p53 transcriptional activity or sensitize p53 to activation by the therapeutic drugs doxorubicin and actinomycin D. We provide evidence that Mdm2 is responsible, at least in part, for repression of the transcriptional activity of the accumulated p53. In MCF7 cells levels of UbcH5B/C are reduced by doxorubicin and actinomycin D. This observation and the sensitivity of p53 expression to levels of UbcH5B/C raise the possibility that E2 regulation could be involved in signaling pathways that control the stability of p53. Our data indicate that UbcH5B/C are physiological E2s for Mdm2, which make a significant contribution to the maintenance of low levels of p53 and Mdm2 in unstressed cells and that inhibition of p53 ubiquitination and degradation by targeting UbcH5B/C is not sufficient to up-regulate p53 transcriptional activity.
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UbcH5-B and UbcH5-C contribute to Mdm2-dependent ubiquitylation and degradation of p53.
“In vitro and in vivo evaluation of a subset of E2 enzymes indicates that UbcH5-B and –C contribute to Mdm2-dependent ubiquitylation and degradation of p53 [24].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [24]
Multiple E2 enzymes can attach ubiquitin to p53 in vitro.
“Although several E2s can transfer ubiquitin to p53 in vitro 118,119”
From MDM2, MDMX and p53 in oncogenesis and cancer therapy (2013) · cites this paper as [119]
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- Authors
- Saville, M. K., Sparks, A., Xirodimas, D. P., Wardrop, J., Stevenson, L. F., Bourdon, J.-C., Woods, Y. L., & Lane, D. P.
- Affiliations
- University of Dundee (GB)
- Corresponding author
- Saville, Mark K.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-10
- Volume
- 279
- Issue
- 40
- Pages
- 42169-42181
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2014396761
- Cited by
- 158
- References
- 79
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 5 · 2023: 9 · 2022: 8 · 2021: 11 · 2020: 5 · 2019: 7 · 2018: 4 · 2017: 2 · 2016: 7 · 2015: 5 · 2014: 7 · 2013: 12 · 2012: 8
- FWCI
- 3.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- 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
- p53, UbcH5b, UbcH5c, UbcH5a, E2 ubiquitin-conjugating enzyme, MDM2, p53 ubiquitination, p53 degradation, 26S proteasome, E3 ubiquitin ligase, p53 transcriptional activity, doxorubicin, actinomycin D, MCF-7 cells, protein stability
- MeSH terms
- Dactinomycin, Doxorubicin, Female, Gene Expression Regulation, Humans, Nuclear Proteins, Protein Processing, Post-Translational, Proto-Oncogene Proteins, Stress, Physiological, Substrate Specificity, Transcription, Genetic, Tumor Suppressor Protein p53, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Cell Line, Tumor, Proto-Oncogene Proteins c-mdm2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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