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Article

Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity.

Cell - 9 Jul 2004

Xirodimas Dimitris P, Saville Mark K, Bourdon Jean-Christophe, Hay Ronald T, Lane David P

Abstract excerpt

The only reported role for the conjugation of the NEDD8 ubiquitin-like molecule is control of the activity of SCF ubiquitin ligase complexes. Here, we show that the Mdm2 RING finger E3 ubiquitin ligase can also promote NEDD8 modification of the p53 tumor suppressor protein. Mdm2 is itself modified with NEDD8 with very similar characteristics to the autoubiquitination activity of Mdm2. By using a cell line (TS-41)...

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Identifiers

PMID: 15242646
DOI: 10.1016/j.cell.2004.06.016

Genes

NEDD8

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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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Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity.PMID 15242646Read ↗

Auto-ubiquitination of Mdm2 enhances its substrate ubiquitin ligase activity.Semantic proximity Read ↗

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Ubiquitination of p53 at multiple sites in the DNA-binding domain.Semantic proximity Read ↗

Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms.Semantic proximity Read ↗

Mdm2 RING mutation enhances p53 transcriptional activity and p53-p300 interaction.Semantic proximity Read ↗

Functional analysis and consequences of Mdm2 E3 ligase inhibition in human tumor cells.Semantic proximity Read ↗

Association of Ubc9, an E2 ligase for SUMO conjugation, with p53 is regulated by phosphorylation of p53.Semantic proximity Read ↗

MDM2 can promote the ubiquitination, nuclear export, and degradation of p53 in the absence of direct binding.Semantic proximity Read ↗

Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes.Semantic proximity Read ↗

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