Lipid-dependent regulation of the unfolded protein response
Current Opinion in Cell Biology
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Volmer, R., & Ron, D. (2014). Lipid-dependent regulation of the unfolded protein response. Current Opinion in Cell Biology, 33 67-73. https://doi.org/10.1016/j.ceb.2014.12.002
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.
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).
Wellcome Trust (100140/Z/12/Z)
EC FP7 CP (277713)
External DOI: https://doi.org/10.1016/j.ceb.2014.12.002
This record's URL: https://www.repository.cam.ac.uk/handle/1810/246824
Attribution 2.0 UK: England & Wales
Licence URL: http://creativecommons.org/licenses/by/2.0/uk/
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