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Article

Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes.

The Journal of biological chemistry - 20 Dec 2002

Miyauchi Yasuhiro, Yogosawa Satomi, Honda Reiko, Nishida Tamotsu, Yasuda Hideyo

Abstract excerpt

Mdm2, a ubiquitin ligase that acts on p53, is regulated by sumoylation. In the current study, we identify the enzymes responsible for the sumoylation of Mdm2. When mammalian cells are co-transfected with cDNAs encoding Mdm2 and PIAS1 or PIASxbeta (protein inhibitor of activated STAT) as sumoylation enzymes, Mdm2 is highly sumoylated. Mdm2 is also sumoylated in an in vitro system containing PIASxbeta, PIAS1, and...

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Identifiers

PMID: 12393906
DOI: 10.1074/jbc.M208319200

Genes

PIAS1

Variants

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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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Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes.PMID 12393906Read ↗

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Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates.Semantic proximity Read ↗

cIAP2 represses IKKα/β-mediated activation of MDM2 to prevent p53 degradation.Semantic proximity Read ↗

Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors.Semantic proximity Read ↗

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