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Article

A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function.

The Journal of cell biology - 4 Dec 2006

Amerik Alexander, Sindhi Nazia, Hochstrasser Mark

Abstract excerpt

Enzyme specificity in vivo is often controlled by subcellular localization. Yeast Doa4, a deubiquitylating enzyme (DUB), removes ubiquitin from membrane proteins destined for vacuolar degradation. Doa4 is recruited to the late endosome after ESCRT-III (endosomal sorting complex required for transport III) has assembled there. We show that an N-terminal segment of Doa4 is sufficient for endosome association. This...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17145966
DOI: 10.1083/jcb.200605134
PMCID: PMC2064681

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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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A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function.PMID 17145966Read ↗

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