Authors: Vanya I Rasheva Pedro M Domingos
Publish Date: 2009/04/10
Volume: 14, Issue: 8, Pages: 996-1007
Abstract
The endoplasmic reticulum ER is the cell organelle where secretory and membrane proteins are synthesized and folded Correctly folded proteins exit the ER and are transported to the Golgi and other destinations within the cell but proteins that fail to fold properly—misfolded proteins—are retained in the ER and their accumulation may constitute a form of stress to the cell—ER stress Several signaling pathways collectively known as unfolded protein response UPR have evolved to detect the accumulation of misfolded proteins in the ER and activate a cellular response that attempts to maintain homeostasis and a normal flux of proteins in the ER In certain severe situations of ER stress however the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis Most research on the UPR used yeast or mammalian model systems and only recently Drosophila has emerged as a system to study the molecular and cellular mechanisms of the UPR Here we review recent advances in Drosophila UPR research in the broad context of mammalian and yeast literature
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