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Abstract
The protein kinase PERK couples protein folding in the endoplasmic reticulum (ER)
to polypeptide biosynthesis by phosphorylating the alpha subunit of eukaryotic translation
initiation factor 2 (eIF2alpha), attenuating translation initiation in response to
ER stress. PERK is highly expressed in mouse pancreas, an organ active in protein
secretion. Under physiological conditions, PERK was partially activated, accounting
for much of the phosphorylated eIF2alpha in the pancreas. The exocrine and endocrine
pancreas developed normally in Perk-/- mice. Postnatally, ER distention and activation
of the ER stress transducer IRE1alpha accompanied increased cell death and led to
progressive diabetes mellitus and exocrine pancreatic insufficiency. These findings
suggest a special role for translational control in protecting secretory cells from
ER stress.