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REVIEW

Endoplasmic Reticulum Stress: Signaling the Unfolded Protein Response

Elida Lai^*, Tracy Teodoro^* and Allen Volchuk

Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network; and Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada avolchuk{at}uhnres.utoronto.ca

The endoplasmic reticulum (ER) is the cellular site of newly synthesized secretory and membrane proteins. Such proteins must be properly folded and posttranslationally modified before exit from the organelle. Proper protein folding and modification requires molecular chaperone proteins as well as an ER environment conducive for these reactions. When ER lumenal conditions are altered or chaperone capacity is overwhelmed, the cell activates signaling cascades that attempt to deal with the altered conditions and restore a favorable folding environment. Such alterations are referred to as ER stress, and the response activated is the unfolded protein response (UPR). When the UPR is perturbed or not sufficient to deal with the stress conditions, apoptotic cell death is initiated. This review will examine UPR signaling that results in cell protective responses, as well as the mechanisms leading to apoptosis induction, which can lead to pathological states due to chronic ER stress.

^* E. Lai and T. Teodoro contributed equally to this review.

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