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• W2947719831 abstract "Endoplasmic reticulum (ER) homeostasis is essential for cell function. Increasing evidence indicates that, efficient protein ER export is important for ER homeostasis. However, the consequence of impaired ER export remains largely unknown. Herein, we found that defective ER protein transport caused by either Sar1 mutants or brefeldin A impaired proinsulin oxidative folding in the ER of β-cells. Misfolded proinsulin formed aberrant disulfide-linked dimers and high molecular weight proinsulin complexes, and induced ER stress. Limiting proinsulin load to the ER alleviated ER stress, indicating that misfolded proinsulin is a direct cause of ER stress. This study revealed significance of efficient ER export in maintaining ER protein homeostasis and native folding of proinsulin. Given the fact that proinsulin misfolding plays an important role in diabetes, this study suggests that enhancing ER export may be a potential therapeutic target to prevent/delay β-cell failure caused by proinsulin misfolding and ER stress." @default.
• W2947719831 created "2019-06-07" @default.
• W2947719831 creator A5010424086 @default.
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• W2947719831 date "2019-08-01" @default.
• W2947719831 modified "2023-10-18" @default.
• W2947719831 title "Defective endoplasmic reticulum export causes proinsulin misfolding in pancreatic β cells" @default.
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• W2947719831 doi "https://doi.org/10.1016/j.mce.2019.110470" @default.
• W2947719831 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6613978" @default.
• W2947719831 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31158417" @default.
• W2947719831 hasPublicationYear "2019" @default.
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