ER stress protects from retinal degeneration |
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Authors: | Clémence Levet Gilles Chatelain Pierre Dourlen Antoine Fouillet Marie‐Laure Dichtel‐Danjoy Alexis Gambis Hyung Don Ryoo Hermann Steller Bertrand Mollereau |
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Institution: | 1. LBMC, UMR5239 CNRS/Ecole Normale Supérieure de Lyon, IFR 128 Biosciences Lyon Gerland, Université de Lyon, Lyon, France;2. Howard Hughes Medical Institute, The Rockefeller University, New York, NY, USA;3. Department of Cell Biology, New York University School of Medicine, New York, NY, USA |
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Abstract: | The unfolded protein response (UPR) is a specific cellular process that allows the cell to cope with the overload of unfolded/misfolded proteins in the endoplasmic reticulum (ER). ER stress is commonly associated with degenerative pathologies, but its role in disease progression is still a matter for debate. Here, we found that mutations in the ER‐resident chaperone, neither inactivation nor afterpotential A (NinaA), lead to mild ER stress, protecting photoreceptor neurons from various death stimuli in adult Drosophila. In addition, Drosophila S2 cultured cells, when pre‐exposed to mild ER stress, are protected from H2O2, cycloheximide‐ or ultraviolet‐induced cell death. We show that a specific ER‐mediated signal promotes antioxidant defences and inhibits caspase‐dependent cell death. We propose that an immediate consequence of the UPR not only limits the accumulation of misfolded proteins but also protects tissues from harmful exogenous stresses. |
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Keywords: | apoptosis cyclophilin Drosophila photoreceptor neuron unfolded protein response |
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