N-terminal polyubiquitination and degradation of the Arf tumor suppressor.

doi:10.1101/gad.1213904

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Article

N-terminal polyubiquitination and degradation of the Arf tumor suppressor.

Genes & development - 1 Aug 2004

Kuo Mei-Ling, den Besten Willem, Bertwistle David, Roussel Martine F, Sherr Charles J

Abstract excerpt

Unknown mechanisms govern degradation of the p19Arf tumor suppressor, an activator of p53 and inhibitor of ribosomal RNA processing. Kinetic metabolic labeling of cells with [3H]-leucine indicated that p19Arf is a relatively stable protein (half-life approximately 6 h) whose degradation depends upon the ubiquitin-proteasome pathway. Although p19Arf binds to the Mdm2 E3 ubiquitin protein ligase to activate p53,...

Topics

Acetylation
Amino Acid Sequence
Animals
Cyclin-Dependent Kinase Inhibitor p16
Cysteine Endopeptidases
Genes, Tumor Suppressor
Genes, p16
Humans
Leucine
Mice
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Multienzyme Complexes

Mutation

NIH 3T3 Cells

Nuclear Proteins

Nucleophosmin

Proteasome Endopeptidase Complex

Proto-Oncogene Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 15289458
DOI: 10.1101/gad.1213904
PMCID: PMC517406

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-15289458-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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