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ER stress protects from retinal degeneration
Author(s) -
Mendes César S,
Levet Clémence,
Chatelain Gilles,
Dourlen Pierre,
Fouillet Antoine,
DichtelDanjoy MarieLaure,
Gambis Alexis,
Ryoo Hyung Don,
Steller Hermann,
Mollereau Bertrand
Publication year - 2009
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2009.76
Subject(s) - unfolded protein response , endoplasmic reticulum , biology , programmed cell death , microbiology and biotechnology , retinal degeneration , chaperone (clinical) , proteotoxicity , proteostasis , cell , protein folding , retinal , apoptosis , genetics , biochemistry , pathology , medicine
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.