Shengyi Sun

Apr 15, 2024 | nature.com | Liangguang Lin |Xiaoqiong Wei |You Lu |Hancheng Mao |Zhen Zhao |Shengyi Sun

Correction to: Nature Communications https://doi.org/10.1038/s41467-024-45633-0, published online 16 February 2024The original version of this Article omitted a reference to previous work in ‘Wei, X., Lu, Y., Lin, L.L. et al. Proteomic screens of SEL1L-HRD1 ER-associated degradation substrates reveal its role in glycosylphosphatidylinositol-anchored protein biogenesis. Nat Commun 15, 659 (2024). https://doi.org/10.1038/s41467-024-44948-2’.

Feb 15, 2024 | nature.com | Liangguang Lin |Xiaoqiong Wei |You Lu |Hancheng Mao |Zhen Zhao |Shengyi Sun

AbstractThe SEL1L-HRD1 protein complex represents the most conserved branch of endoplasmic reticulum (ER)-associated degradation (ERAD). Despite recent advances in both mouse models and humans, in vivo evidence for the importance of SEL1L in the ERAD complex formation and its (patho-)physiological relevance in mammals remains limited.