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Lipid-dependent regulation of the unfolded protein response.


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Type

Article

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Authors

Volmer, Romain 

Abstract

Protein folding homeostasis in the lumen of the endoplasmic reticulum is defended by signal transduction pathways that are activated by an imbalance between unfolded proteins and chaperones (so called ER stress). Collectively referred to as the unfolded protein response (UPR) this homeostatic response is initiated by three known ER stress transducers: IRE1, PERK and ATF6. These ER-localised transmembrane (TM) proteins posses lumenal stress sensing domains and cytosolic effector domains that collectively activate a gene expression programme regulating the production of proteins involved in the processing and maturation of secreted proteins that enter the ER. However, beyond limiting unfolded protein stress in the ER the UPR has important connections to lipid metabolism that are the subject of this review.

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Keywords

Animals, Endoplasmic Reticulum, Eukaryota, Humans, Lipid Metabolism, Molecular Chaperones, Protein Folding, Signal Transduction, Unfolded Protein Response

Journal Title

Curr Opin Cell Biol

Conference Name

Journal ISSN

0955-0674
1879-0410

Volume Title

33

Publisher

Elsevier BV
Sponsorship
Wellcome Trust (100140/Z/12/Z)
European Commission (277713)
This work was supported by a Wellcome Trust Intermediate Clinical Fellowship (to R.V.), a Wellcome Trust Principal Research Fellowship (to D.R.), and European Union Seventh Framework Programme Grant (Beta Bat, 277713).