ER stress protects from retinal degeneration

César S. Mendes, Clémence Levet, Gilles Chatelain, Pierre Dourlen, Antoine Fouillet, Marie Laure Dichtel-Danjoy, Alexis Gambis, Hyung Don Ryoo, Hermann Steller, Bertrand Mollereau

Research output: Contribution to journalArticlepeer-review


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"2O"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.

Original languageEnglish (US)
Pages (from-to)1296-1307
Number of pages12
JournalEMBO Journal
Issue number9
StatePublished - May 6 2009


  • Apoptosis
  • Cyclophilin
  • Drosophila
  • Photoreceptor neuron
  • Unfolded protein response

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology


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