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Article

Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding.

Molecular and cellular biology - 1 Apr 2011

Böhm Stefanie, Lamberti Giorgia, Fernández-Sáiz Vanesa, Stapf Christopher, Buchberger Alexander

Abstract excerpt

The chaperone-related AAA ATPase Cdc48 (p97/VCP in higher eukaryotes) segregates ubiquitylated proteins for subsequent degradation by the 26S proteasome or for nonproteolytic fates. The specific outcome of Cdc48 activity is controlled by the evolutionary conserved cofactors Ufd2 and Ufd3, which antagonistically regulate the substrates' ubiquitylation states. In contrast to the interaction of Ufd3 and Cdc48, the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Proteasome Endopeptidase Complex

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Source

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Identifiers

PMID: 21282470
DOI: 10.1128/MCB.00962-10
PMCID: PMC3135295

Genes

VCP

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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Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding.PMID 21282470Read ↗

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