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Protein Disulfide Isomerase A6 Controls the Decay of IRE1 alpha Signaling via Disulfide-Dependent Association
Journal article   Open access   Peer reviewed

Protein Disulfide Isomerase A6 Controls the Decay of IRE1 alpha Signaling via Disulfide-Dependent Association

Davide Eletto, Daniela Eletto, Devin Dersh, Tali Gidalevitz and Yair Argon
Molecular cell, v 53(4), pp 562-576
20 Feb 2014
PMID: 24508390
url
https://doi.org/10.1016/j.molcel.2014.01.004View
Published, Version of Record (VoR)Open Access (Publisher-Specific) Open

Abstract

Biochemistry & Molecular Biology Cell Biology Life Sciences & Biomedicine Science & Technology
The response to endoplasmic reticulum (ER) stress relies on activation of unfolded protein response (UPR) sensors, and the outcome of the UPR depends on the duration and strength of signal. Here, we demonstrate a mechanism that attenuates the activity of the UPR sensor inositol-requiring enzyme 1 alpha (IRE1 alpha). A resident ER protein disulfide isomerase, PDIA6, limits the duration of IRE1 alpha activity by direct binding to cysteine 148 in the lumenal domain of the sensor, which is oxidized when IRE1 is activated. PDIA6-deficient cells hyperrespond to ER stress with sustained autophosphorylation of IRE1 alpha and splicing of XBP1 mRNA, resulting in exaggerated upregulation of UPR target genes and increased apoptosis. In vivo, PDIA6-deficient C. elegans exhibits constitutive UPR and fails to complete larval development, a program that normally requires the UPR. Thus, PDIA6 activity provides a mechanism that limits UPR signaling and maintains it within a physiologically appropriate range.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
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