Functional rescue of a disease-linked ERAD pathway mutation via alternative splicing
Huilun Helen Wang·Ling Qi·Zexin Jason Li·Zhihong Wang·Sunil K Verma·Lulu Jiang·Weronika Gniadzik·Hui Ming Wang·Liangguang Leo Lin·Muge N Kuyumcu-Martinez·Emily Whitestone·Shengyi Sun
ER-associated degradation (ERAD) targets misfolded proteins in the endoplasmic reticulum (ER) for proteasomal degradation. Mutations in its most conserved branch involving the SEL1L-HRD1 complex cause ERAD-associated neurodevelopmental disorders with onset in infancy (ENDI), characterized by developmental delay, microcephaly, and locomotor dysfunction. Its most severe form, ENDI with agammaglobulinemia (ENDI-A), results from a bi-allelic SEL1L-Cys141Tyr (C141Y) mutation within its fibronectin II
