ER Stress Protects from Retinal Degeneration

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 2009 Apr 3

PMID 19339992

Citations 69

Authors

Cesar S Mendes

Clemence Levet

Gilles Chatelain

Pierre Dourlen

Antoine Fouillet

Marie-Laure Dichtel-Danjoy

Alexis Gambis

Hyung Don Ryoo

Hermann Steller

Bertrand Mollereau

Affiliations

Soon will be listed here.

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.

Citing Articles

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