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Exploring Cellular Stress Response and Chaperones

Overview
Journal Cells
Publisher MDPI
Date 2019 May 5
PMID 31052568
Citations 7
Authors
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Abstract

Since the pioneering discovery of heat shock proteins in by Ferruccio Ritossa in 1960s, a long and exciting journey has been undertaken by molecular biologists and researchers worldwide. Not only lower organisms like worms, yeast, amoeba, and flies but also eukaryotes share common cellular response signals to stressful conditions that can arise from the outside but also from the inside. Moreover, extraordinary interplay between nucleus and subcellular organelles, and between different organelles, like mitochondria and the endoplasmic reticulum called mitochondria-associated endoplasmic reticulum membranes (MAMs), are involved in aging and human diseases like obesity, diabetes, inflammation, neurodegeneration, autoimmune diseases, atherosclerosis, and cancer. Actually, we know that to hit abnormal proteostasis and lipid exchanges in the endoplasmic reticulum is crucial to best guide effective therapies or discover new drugs. Indeed, restoration or impairment of endoplasmic reticulum shape and function lead to cellular homeostasis by autophagy or to final death generally by apoptosis or pyroptosis. This Special Issue collects current valuable articles or reviews on cellular stress research and each contribution opens a new window for further studies and hypothesis. I hope that readers interested in this fascinating topic may be stimulated to know more and more.

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References
1.
Kawasaki N, Asada R, Saito A, Kanemoto S, Imaizumi K . Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue. Sci Rep. 2012; 2:799. PMC: 3495279. DOI: 10.1038/srep00799. View

2.
Bravo R, Parra V, Gatica D, Rodriguez A, Torrealba N, Paredes F . Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration. Int Rev Cell Mol Biol. 2013; 301:215-90. PMC: 3666557. DOI: 10.1016/B978-0-12-407704-1.00005-1. View

3.
Palade G . The endoplasmic reticulum. J Biophys Biochem Cytol. 1956; 2(4 Suppl):85-98. PMC: 2229739. DOI: 10.1083/jcb.2.4.85. View

4.
Dominguez-Martin E, Hernandez-Elvira M, Vincent O, Coria R, Escalante R . Unfolding the Endoplasmic Reticulum of a Social Amoeba: as a New Model for the Study of Endoplasmic Reticulum Stress. Cells. 2018; 7(6). PMC: 6025073. DOI: 10.3390/cells7060056. View

5.
Upton J, Wang L, Han D, Wang E, Huskey N, Lim L . IRE1α cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2. Science. 2012; 338(6108):818-22. PMC: 3742121. DOI: 10.1126/science.1226191. View