Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 2. Protein misfolding and ER stress.
Accepted version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Chambers, Joseph E
Marciniak, Stefan J
Abstract
The endoplasmic reticulum (ER) is a major site of protein synthesis, most strikingly in the specialized secretory cells of metazoans, which can produce their own weight in proteins daily. Cells possess a diverse machinery to ensure correct folding, assembly, and secretion of proteins from the ER. When this machinery is overwhelmed, the cell is said to experience ER stress, a result of the accumulation of unfolded or misfolded proteins in the lumen of the organelle. Here we discuss the causes of ER stress and the mechanisms by which cells elicit a response, with an emphasis on recent discoveries.
Description
Keywords
ATF6, ER stress, IRE1, PERK, UPR, Animals, Endoplasmic Reticulum Stress, Endoplasmic Reticulum-Associated Degradation, Heat-Shock Proteins, Humans, Oxidative Stress, Protein Folding, Proteolysis, Proteostasis Deficiencies, Signal Transduction
Journal Title
Am J Physiol Cell Physiol
Conference Name
Journal ISSN
0363-6143
1522-1563
1522-1563
Volume Title
307
Publisher
American Physiological Society
Publisher DOI
Sponsorship
Medical Research Council (G1002610)
Medical Research Council (G0601840)
Wellcome Trust (100140/Z/12/Z)
Medical Research Council (G0601840)
Wellcome Trust (100140/Z/12/Z)