Cited by 77Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysHeat shock proteins research

Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase

Okamoto, Koji, Taya, Yoichi, Nakagama, Hitoshi·2009·FEBS Letters

Abstract

mdm2 and mdmx oncogenes play essential yet non-redundant roles in synergistic inactivation of the tumor suppressor, p53. While Mdm2 inhibits p53 activity mainly by augmenting its ubiquitination, the functional role of Mdmx on p53 ubiquitination remains obscure. In transfected H1299 cells, Mdmx augmented Mdm2-mediated ubiquitination of p53. In in vitro ubiquitination assays, the Mdmx/Mdm2 heteromeric complex, in comparison to the Mdm2 homomer, showed enhanced ubiquitinase activity toward p53 and the reduced auto-ubiquitination of Mdm2. Alteration of the substrate specificity via binding to Mdmx may contribute to efficient ubiquitination and inactivation of p53 by Mdm2.

Integrity signals

Registry

Crossref · 10.1016/j.febslet.2009.07.021

Cites

38 of 38 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Mdm2's substrate specificity is switched from itself towards p53 upon Mdmx binding.

    “By contrast, Mdm2’s substrate specificity is switched from itself towards p53 upon Mdmx binding [42].”

    From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [42]

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Okamoto, K., Taya, Y., & Nakagama, H.
Affiliations
  • Japan Science and Technology Agency (JP)
  • National Cancer Center Research Institute (JP)
Corresponding author
Nakagama, Hitoshi
Venue
FEBS Letters
Publisher
Wiley
Published
2009-07-18
Volume
583
Issue
17
Pages
2710-2714
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2017557952
Cited by
76
References
38
Citations by year
2024: 4 · 2022: 5 · 2021: 2 · 2020: 4 · 2019: 1 · 2017: 3 · 2016: 5 · 2015: 4 · 2014: 10 · 2013: 9 · 2012: 13
FWCI
4.80
Type
journal article
Language
en
Open access
closed
Locations
  • FEBS Letters (publishedVersion)
  • PubMed (publishedVersion)
  • Institutional Repositories DataBase (IRDB) (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
MDMX, MDM2, p53, ubiquitination, E3 ubiquitin ligase, substrate specificity, p53 inactivation, tumor suppressor regulation
MeSH terms
Humans, Nuclear Proteins, Proto-Oncogene Proteins, Substrate Specificity, Tumor Suppressor Protein p53, Cell Cycle Proteins, Cell Line, Tumor, Proto-Oncogene Proteins c-mdm2, Ubiquitination

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 ›

Are you an author, or do you see a problem with this page? Request a review