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Article

A role for mammalian Ubc6 homologues in ER-associated protein degradation.

Journal of cell science - 15 Jul 2002

Lenk Uwe, Yu Helen, Walter Jan, Gelman Marina S, Hartmann Enno, Kopito Ron R, Sommer Thomas

Abstract excerpt

Integral membrane and secretory proteins which fail to fold productively are retained in the endoplasmic reticulum and targeted for degradation by cytoplasmic proteasomes. Genetic and biochemical analyses suggest that substrates of this pathway must be dislocated across the membrane of the endoplasmic reticulum (ER) by a process requiring a functional Sec61 complex and multiubiquitinylation. In yeast, the...

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Identifiers

PMID: 12082160
DOI: 10.1242/jcs.115.14.3007

Genes

CFTR

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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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A role for mammalian Ubc6 homologues in ER-associated protein degradation.PMID 12082160Read ↗

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Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508.Semantic proximity Read ↗

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A regulatory link between ER-associated protein degradation and the unfolded-protein response.Semantic proximity Read ↗

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