Lipid-dependent regulation of the unfolded protein response

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 respon...

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Bibliographic Details
Published inCurrent opinion in cell biology Vol. 33; pp. 67 - 73
Main Authors Volmer, Romain, Ron, David
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.04.2015
Elsevier
Subjects
Animals
Endoplasmic Reticulum - metabolism
Eukaryota - metabolism
Humans
Internal Medicine
Life Sciences
Lipid Metabolism
Molecular Chaperones - biosynthesis
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Protein Folding
Signal Transduction
Unfolded Protein Response
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Summary: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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PMCID: PMC4376399
ISSN:0955-0674
1879-0410
1879-0410
DOI:10.1016/j.ceb.2014.12.002