|Citation||Mendes, C.S., Levet, C., Chatelain, G., Dourlen, P., Fouillet, A., Dichtel-Danjoy, M.L., Gambis, A., Ryoo, H.D., Steller, H., Mollereau, B. (2009). ER stress protects from retinal degeneration. EMBO J. 28(9): 1296--1307. (Export to RIS)|
|Publication Type||Research paper|
|PubMed 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 H(2)O(2), 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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|Language of Publication||English|
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|Also Published As|
|Title||The EMBO Journal|
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|Natural transposons (1)|