未折叠蛋白反应
蛋白质折叠
内质网
战斗或逃跑反应
压力(语言学)
细胞生物学
化学
生物
生物化学
语言学
基因
哲学
出处
期刊:Cell Reports
[Elsevier]
日期:2024-06-01
卷期号:43 (6): 114358-114358
标识
DOI:10.1016/j.celrep.2024.114358
摘要
Despite the consensus that accumulation of unfolded proteins in the endoplasmic reticulum (ER) lumen, i.e. ER stress, activates the unfolded protein response (UPR), studies under physiological and pathophysiological conditions suggest that ER stress may not always trigger the UPR, and the UPR can be activated in an ER stress-independent way. To better understand how the UPR is regulated and its relationship with ER stress requires direct detection of unfolded proteins in the ER, a method that is still lacking. Here, we report a strategy of visualizing unfolded protein accumulation in the ER lumen in living cells by employing an engineered ER stress sensor, PERK, which forms fluorescence puncta upon unfolded protein binding, in a fast and reversible way. Our reporter enables us to clarify the involvement of unfolded proteins in UPR activation under several physiological conditions and suggests that persistent unfolded protein accumulation in the ER despite UPR attenuation predicts cell death.
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