J Bacteriol Virol.  2012 Sep;42(3):196-202. 10.4167/jbv.2012.42.3.196.

Endoplasmic Reticulum Stress Responses and Apoptosis

• Song CH

• KMID: 1434748
• DOI: http://doi.org/10.4167/jbv.2012.42.3.196

Abstract

The endoplasmic reticulum (ER) plays a crucial role in various cellular activities and cell survival. Almost all of the resident proteins usually enter the ER, and are modified with N-linked glycans and folded into the appropriate secondary and tertiary structures. When cells are faced with stressful conditions, unfolded proteins are accumulated in the ER. The discrepancies between the protein folding capacities and client protein load lead to ER stress. If the stress is prolonged, ER stress responses can activate apoptosis. ER stress-mediated apoptosis is implicated in the pathophysiology of human diseases, including several neurodegenerative diseases, diabetes mellitus, and various infectious diseases. Thus, the ER is now considered as an important organelle that can decide cell survival or death. In this review, the recent progress on ER stress and apoptosis is summarized.

Keyword

ER stress; Apoptosis; Organelle

MeSH Terms

Apoptosis
Cell Survival
Communicable Diseases
Diabetes Mellitus
Endoplasmic Reticulum
Endoplasmic Reticulum Stress
Humans
Neurodegenerative Diseases
Organelles
Polysaccharides
Protein Folding
Proteins
Polysaccharides
Proteins

Figure

• 

  Figure 1 ER stress response and apoptosis. On ER stress, IRE1, PERK, and ATF6 proteins initiate signal transduction that controls cell survival or death. There are at least three different mechanisms to induce ER stress; translational attenuation to avoid further accumulation of misfolded ER proteins; transcriptional activation of genes encoding ER-resident molecular chaperones; and the ER-associated degradation (ERAD) pathway to restore the folding capacity. If the cells are exposed to prolonged and strong ER stress, the damaged cells are destroyed by apoptosis.

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