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Article

A structurally unique E2-binding domain activates ubiquitination by the ERAD E2, Ubc7p, through multiple mechanisms.

Molecular cell - 23 May 2013

Metzger Meredith B, Liang Yu-He, Das Ranabir, Mariano Jennifer, Li Shengjian, Li Jess, Kostova Zlatka, Byrd R Andrew, Ji Xinhua, Weissman Allan M

Abstract excerpt

Cue1p is an integral component of yeast endoplasmic reticulum (ER)-associated degradation (ERAD) ubiquitin ligase (E3) complexes. It tethers the ERAD ubiquitin-conjugating enzyme (E2), Ubc7p, to the ER and prevents its degradation, and also activates Ubc7p via unknown mechanisms. We have now determined the crystal structure of the Ubc7p-binding region (U7BR) of Cue1p with Ubc7p. The U7BR is a unique E2-binding...

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Identifiers

PMID: 23665230
DOI: 10.1016/j.molcel.2013.04.004
PMCID: PMC4109681

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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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