Preprint Review Version 1 This version is not peer-reviewed

Methods for Studying Endoplasmic Reticulum Stress

Version 1 : Received: 6 September 2019 / Approved: 9 September 2019 / Online: 9 September 2019 (11:54:25 CEST)

How to cite: Correia da Silva, D.; Valentao, P.; Andrade, P.; Pereira, D. Methods for Studying Endoplasmic Reticulum Stress. Preprints 2019, 2019090098 (doi: 10.20944/preprints201909.0098.v1). Correia da Silva, D.; Valentao, P.; Andrade, P.; Pereira, D. Methods for Studying Endoplasmic Reticulum Stress. Preprints 2019, 2019090098 (doi: 10.20944/preprints201909.0098.v1).

Abstract

The endoplasmic reticulum (ER) comprises a network of tubules and vesicles that constitutes the largest organelle of the eukaryotic cell. Being the location where most proteins are synthesized and folded, it is crucial for the upkeep of cellular homeostasis. In addition, it is the largest ionic calcium reservoir in cells, tightly regulating the levels of this second messenger according to cellular necessities. Disturbed ER homeostasis triggers the activation of an intricate and conserved molecular machinery, termed the unfolded protein response (UPR). Given the impact of this signaling network upon an extensive list of cellular processes, ER stress is involved in the onset and progression of multiple diseases, including cancer and neurodegenerative disorders. There is, for this reason, an increasing number of publications focused on characterizing and/or modulating ER stress, which have resulted in a wide array of techniques employed to study ER-related molecular events. This review aims to sum up the tools available design a study of this nature.

Subject Areas

unfolded protein response; endoplasmic reticulum; PERK; IRE-1; ATF4

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