2023年9月15日 · ER stress activates an adaptive unfolded protein response to restore proteostasis by initiating protein kinase R-like ER kinase, activating transcription factor 6, and inositol requiring enzyme...

2020年11月19日 · This Review focuses on the common drivers of ER stress in the tumour microenvironment (TME), the interplay between oncogenic events and ER stress responses, and the mechanisms by which ER stress...

We define ER stress by its type of stressor, which is driven by proteotoxicity, lipotoxicity, and/or glucotoxicity. We discuss the implications of ER stress in metabolic disorders by reviewing evidence implicating ER phenotypes and organelle communication, protein quality control, calcium homeostasis, lipid and carbohydrate metabolism, and ...

Our review provides a synthesis of intracellular ER signalling revolving around proteostasis and the UPR, its impact on other organelles and cellular behaviour, its multifaceted and dynamic response to stress and its role in physiology, before finally exploring the potential exploitation of this knowledge to tackle unresolved biological question...

2020年5月26日 · Cellular stress induced by the abnormal accumulation of unfolded or misfolded proteins at the endoplasmic reticulum (ER) is emerging as a possible driver of human diseases, including...

2023年9月15日 · ER stress activates an adaptive unfolded protein response to restore proteostasis by initiating protein kinase R-like ER kinase, activating transcription factor 6, and inositol requiring enzyme 1. ER stress is multifaceted, and acts on aspects at the epigenetic level, including transcription and protein processing.

ER stress occurs when the capacity of the ER to fold proteins becomes saturated. ER stress may be caused by factors that impair protein glycosylation or disulfide bond formation, or by overexpression of or mutations in proteins entering the secretory pathway.

In the absence of ER stress, ER luminal GRP78 associates with ER transmembrane proteins PERK, IRE1, and ATF6 to block their activation (shown as inactive UPR in the top right square). Upon ER stress, accumulating unfolded and misfolded proteins inside the ER sequester GRP78, thus dissociating this master regulator from all three transmembrane ...

The endoplasmic reticulum (ER) stress refers to a condition that unfolded proteins accumulation in ER in response to stimuli such as oxidative stress, metabolic and ischemic insult. ER stress triggers the unfolded protein response (UPR) and activate PKR-like ER kinase (PERK), activating transcription factor 6 (ATF6), and inositol-requiring ...

2013年12月1日 · Perturbations in ER function, a process named “ER-stress”, trigger the unfolded protein response (UPR), a tightly orchestrated collection of intracellular signal transduction reactions designed to restore protein homeostasis.