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Article

Nucleocytoplasmic shuttling of p53 is essential for MDM2-mediated cytoplasmic degradation but not ubiquitination.

Molecular and cellular biology - 1 Sept 2003

O'Keefe Kevin, Li Huiping, Zhang Yanping

Abstract excerpt

As a shuttling protein, p53 is constantly transported through the nuclear pore complex. p53 nucleocytoplasmic transport is carried out by a bipartite nuclear localization signal (NLS) located at its C-terminal domain and two nuclear export signals (NES) located in its N- and C-terminal regions, respectively. The role of nucleocytoplasmic shuttling in p53 ubiquitination and degradation has been a subject of...

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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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Share to Hydrophobic and Hydrophilic Interactions

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Source

Open in PubMed Open full text

Identifiers

PMID: 12944468
DOI: 10.1128/MCB.23.18.6396-6405.2003
PMCID: PMC193719

Genes

MDM2
NES

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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