Article
Structural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core Complex.
Nature communications - 27 Jan 2026
Lin Liangguang Leo, Maldosevic Emir, Zhou Linyao Elina, Jomaa Ahmad, Qi Ling
Abstract excerpt
The SEL1L-HRD1 complex represents the most conserved branch of endoplasmic reticulum (ER)-associated degradation (ERAD), a critical quality-control pathway that clears misfolded ER proteins. However, the molecular organization and pathogenic mechanisms of mammalian ERAD have remained elusive. Here, we report the cryo-EM structure of the core mammalian ERAD complex, comprising the ER lectin OS9, SEL1L, and the E3...
Topics
- Endoplasmic Reticulum-Associated Degradation
- Humans
- Ubiquitin-Protein Ligases
- Lectins
- Endoplasmic Reticulum
- Proteins
- Cryoelectron Microscopy
- Protein Multimerization
- Mutation
- Animals
- HEK293 Cells
- Neoplasm Proteins