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Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death.

Abstract：

:A variety of debilitating diseases including diabetes, Alzheimer's, Huntington's, Parkinson's, and prion-based diseases are linked to stress within the endoplasmic reticulum (ER). Using S. cerevisiae, we sought to determine the relationship between protein misfolding, ER stress, and cell death. In the absence of ERV29, a stress-induced gene required for ER associated degradation (ERAD), misfolded proteins accumulate in the ER leading to persistent ER stress and subsequent cell death. Cells alleviate ER stress through the unfolded protein response (UPR); however, if stress is sustained the UPR contributes to cell death by causing the accumulation of reactive oxygen species (ROS). ROS are generated from two sources: the UPR-regulated oxidative folding machinery in the ER and mitochondria. Our results demonstrate a direct mechanism(s) by which misfolded proteins lead to cellular damage and death.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Haynes CM,Titus EA,Cooper AA

doi

10.1016/j.molcel.2004.08.025

subject

Has Abstract

pub_date

2004-09-10 00:00:00

pages

767-76

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(04)00511-8

journal_volume

15

pub_type

杂志文章

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