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Article

The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast.

Molecular biology of the cell - 1 Aug 1999

Swaminathan S, Amerik A Y, Hochstrasser M

Abstract excerpt

Attachment of ubiquitin to cellular proteins frequently targets them to the 26S proteasome for degradation. In addition, ubiquitination of cell surface proteins stimulates their endocytosis and eventual degradation in the vacuole or lysosome. In the yeast Saccharomyces cerevisiae, ubiquitin is a long-lived protein, so it must be efficiently recycled from the proteolytic intermediates to which it becomes linked....

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Identifiers

PMID: 10436014
DOI: 10.1091/mbc.10.8.2583
PMCID: PMC25490

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast.PMID 10436014Read ↗

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Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway.Semantic proximity Read ↗

A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function.Semantic proximity Read ↗

Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

The DOA pathway: studies on the functions and mechanisms of ubiquitin-dependent protein degradation in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Inactivation of the VID27 gene prevents suppression of the doa4 degradation defect in doa4Δ did3Δ double mutant.Semantic proximity Read ↗

The structure and function of deubiquitinases: lessons from budding yeastSemantic proximity Read ↗

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