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Amyloid beta regulates ER exit sites formation through O‐GlcNAcylation triggered by disrupted calcium homeostasis

Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease. Calcium is required for the fusion and trafficking of vesicles. Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O‐GlcNAcylation. O‐GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.