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• W2068854526 abstract "Loss-of-function mutations in EIF2AK3, encoding the pancreatic endoplasmic reticulum (ER) kinase, PERK, are associated with dysfunction of the endocrine pancreas and diabetes. However, to date it has not been possible to uncouple the long term developmental effects of PERK deficiency from sensitization to physiological levels of ER unfolded protein stress upon interruption of PERK modulation of protein synthesis rates. Here, we report that a selective PERK inhibitor acutely deregulates protein synthesis in freshly isolated islets of Langerhans, across a range of glucose concentrations. Acute loss of the PERK-mediated strand of the unfolded protein response leads to rapid accumulation of misfolded pro-insulin in cultured beta cells and is associated with a kinetic defect in pro-insulin processing. These in vitro observations uncouple the latent role of PERK in beta cell development from the regulation of unfolded protein flux through the ER and attest to the importance of the latter in beta cell proteostasis." @default.
• W2068854526 created "2016-06-24" @default.
• W2068854526 creator A5002076790 @default.
• W2068854526 creator A5010360422 @default.
• W2068854526 creator A5077934127 @default.
• W2068854526 date "2012-12-01" @default.
• W2068854526 modified "2023-10-14" @default.
• W2068854526 title "Uncoupling Proteostasis and Development in Vitro with a Small Molecule Inhibitor of the Pancreatic Endoplasmic Reticulum Kinase, PERK" @default.
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• W2068854526 doi "https://doi.org/10.1074/jbc.m112.428987" @default.
• W2068854526 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3531748" @default.
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• W2068854526 hasPublicationYear "2012" @default.
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