The UPR ER : Sensor and Coordinator of Organismal Homeostasis

Life is stressful. Organisms are repeatedly exposed to stressors that disrupt protein homeostasis (proteostasis), resulting in protein misfolding and aggregation. To sense and respond to proteotoxic perturbations, cells have evolved compartment-specific stress responses, such as the unfolded protein...

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Bibliographic Details
Published in:Molecular cell 2017-06, Vol.66 (6), p.761-771
Main Authors: Frakes, Ashley E, Dillin, Andrew
Format: Article
Language:English
Subjects:
Aging - metabolism
Aging - pathology
Amyotrophic Lateral Sclerosis - metabolism
Amyotrophic Lateral Sclerosis - pathology
Animals
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum - pathology
Endoplasmic Reticulum Stress
Homeostasis
Humans
Inflammation - metabolism
Inflammation - pathology
Inflammation Mediators
NF-kappa B - metabolism
Protein Aggregates
Signal Transduction
Unfolded Protein Response
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Summary:Life is stressful. Organisms are repeatedly exposed to stressors that disrupt protein homeostasis (proteostasis), resulting in protein misfolding and aggregation. To sense and respond to proteotoxic perturbations, cells have evolved compartment-specific stress responses, such as the unfolded protein response of the endoplasmic reticulum (UPR ). However, UPR function is impaired with age, which, we propose, creates a permissive environment for protein aggregation, unresolved ER stress, and chronic inflammation. Understanding age-related changes to the UPR will provide new avenues for therapeutic intervention in metabolic disease, neurodegeneration, and aging.
ISSN:1097-2765
1097-4164
DOI:10.1016/j.molcel.2017.05.031