title: ER stress protects from retinal degeneration.
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.
authors.affiliation: Howard Hughes Medical Institute, The Rockefeller University, New York, NY, USA.
authors.forename: César S
authors.initials: CS
authors.lastname: Mendes
authors.forename: Clémence
authors.initials: C
authors.lastname: Levet
authors.forename: Gilles
authors.initials: G
authors.lastname: Chatelain
authors.forename: Pierre
authors.initials: P
authors.lastname: Dourlen
authors.forename: Antoine
authors.initials: A
authors.lastname: Fouillet
authors.forename: Marie-Laure
authors.initials: ML
authors.lastname: Dichtel-Danjoy
authors.forename: Alexis
authors.initials: A
authors.lastname: Gambis
authors.forename: Hyung Don
authors.initials: HD
authors.lastname: Ryoo
authors.forename: Hermann
authors.initials: H
authors.lastname: Steller
authors.forename: Bertrand
authors.initials: B
authors.lastname: Mollereau