Lipid-dependent regulation of the unfolded protein response

Romain Volmer (1, 2, 3, 4) , David Ron (2, 3, 4)

1 IHAP - Interactions hôtes-agents pathogènes [Toulouse]
2 CIMR - Cambridge Institute for Medical Research
3 Wellcome Trust-MRC Institute of Metabolic Science
4 CAM - University of Cambridge [UK]

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.

Domaines: Sciences du Vivant [q-bio]

Romain Volmer, David Ron. Lipid-dependent regulation of the unfolded protein response. Current Opinion in Cell Biology, 2015, 33, pp.67-73. ⟨10.1016/j.ceb.2014.12.002⟩. ⟨hal-02637534⟩