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Article

C-terminal ubiquitination of p53 contributes to nuclear export.

Molecular and cellular biology - 1 Dec 2001

Lohrum M A, Woods D B, Ludwig R L, Bálint E, Vousden K H

Abstract excerpt

The growth inhibitory functions of p53 are controlled in unstressed cells by rapid degradation of the p53 protein. One of the principal regulators of p53 stability is MDM2, a RING finger protein that functions as an E3 ligase to ubiquitinate p53. MDM2 promotes p53 nuclear export, and in this study, we show that ubiquitination of the C terminus of p53 by MDM2 contributes to the efficient export of p53 from the...

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Share to Active Transport, Cell Nucleus
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 11713287
DOI: 10.1128/MCB.21.24.8521-8532.2001
PMCID: PMC100015

Genes

MDM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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C-terminal ubiquitination of p53 contributes to nuclear export.PMID 11713287Read ↗

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