Endoplasmic Reticulum Stress Responses and Apoptosis

Chang-Hwa Song

doi:10.4167/jbv.2012.42.3.196

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Song: Endoplasmic Reticulum Stress Responses and Apoptosis

Review Article

Journal of Bacteriology and Virology

Journal of Bacteriology and Virology 2012; 42(3): 196-202.

Published online: 24 September 2012

DOI: https://doi.org/10.4167/jbv.2012.42.3.196

Endoplasmic Reticulum Stress Responses and Apoptosis

Chang-Hwa Song

Department of Microbiology and Research Institute for Medical Sciences, College of Medicine, Chungnam National University, Daejeon, Korea.

Corresponding author: Dr. Chang-Hwa Song. Department of Microbiology, College of Medicine, Chungnam National University, 6 Munhwa-dong, Junggu, Daejeon 301-747, Korea. Phone: +82-42-580-8245, Fax: +82-42-585-3686, songch@cnu.ac.kr

Received 27 May 2012 Revised 27 June 2012 Accepted 2 July 2012

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.

Keywords: ER stress, Apoptosis, Organelle

Figures and Tables

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.

Notes

This work was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2010-0008352), and by the National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (No. 2011-0027459).

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