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Article

Wild-type and cancer-related p53 proteins are preferentially degraded by MDM2 as dimers rather than tetramers.

Genes & development - 1 Mar 2018

Katz Chen, Low-Calle Ana Maria, Choe Joshua H, Laptenko Oleg, Tong David, Joseph-Chowdhury Jazmine-Saskya N, Garofalo Francesca, Zhu Yan, Friedler Assaf, Prives Carol

Abstract excerpt

The p53 tumor suppressor protein is the most well studied as a regulator of transcription in the nucleus, where it exists primarily as a tetramer. However, there are other oligomeric states of p53 that are relevant to its regulation and activities. In unstressed cells, p53 is normally held in check by MDM2 that targets p53 for transcriptional repression, proteasomal degradation, and cytoplasmic localization. Here...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proteasome Endopeptidase Complex

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Share to Proto-Oncogene Proteins c-mdm2

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Source

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Identifiers

PMID: 29549180
DOI: 10.1101/gad.304071.117
PMCID: PMC5900715

Genes

MDM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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