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Article

'ER degradation' of a mutant yeast plasma membrane protein by the ubiquitin-proteasome pathway.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Mar 1998

Galan J M, Cantegrit B, Garnier C, Namy O, Haguenauer-Tsapis R

Abstract excerpt

The yeast plasma membrane, uracil permease, undergoes ubiquitin-dependent endocytosis and subsequent degradation in the vacuole via a process that does not involve the proteasome. Cell-surface ubiquitination of this protein is mediated by the ubiquitin-protein ligase Npi1p/Rsp5p and involves Lys6...

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Identifiers

PMID: 9506475
DOI: 10.1096/fasebj.12.3.315

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-9506475-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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'ER degradation' of a mutant yeast plasma membrane protein by the ubiquitin-proteasome pathway.PMID 9506475Read ↗

Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein.Semantic proximity Read ↗

Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease.Semantic proximity Read ↗

Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease.Semantic proximity Read ↗

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Systematic mutational analysis of the intracellular regions of yeast Gap1 permease.Semantic proximity Read ↗

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The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies.Semantic proximity Read ↗

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