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Mechanisms, regulation and functions of the unfolded protein response.
Nature Reviews Molecular Cell Biology ( IF 112.7 ) Pub Date : 2020-05-26 , DOI: 10.1038/s41580-020-0250-z
Claudio Hetz 1, 2, 3, 4 , Kezhong Zhang 5, 6 , Randal J Kaufman 7
Affiliation  

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 cancer, diabetes, obesity and neurodegeneration. ER proteostasis surveillance is mediated by the unfolded protein response (UPR), a signal transduction pathway that senses the fidelity of protein folding in the ER lumen. The UPR transmits information about protein folding status to the nucleus and cytosol to adjust the protein folding capacity of the cell or, in the event of chronic damage, induce apoptotic cell death. Recent advances in the understanding of the regulation of UPR signalling and its implications in the pathophysiology of disease might open new therapeutic avenues.



中文翻译:

未折叠蛋白反应的机制、调控和功能。

由内质网 (ER) 处未折叠或错误折叠蛋白质的异常积累引起的细胞应激正在成为人类疾病的可能驱动因素,包括癌症、糖尿病、肥胖和神经退行性疾病。ER 蛋白稳态监测由未折叠蛋白反应 (UPR) 介导,UPR 是一种信号转导途径,可感知 ER 腔中蛋白质折叠的保真度。UPR 将有关蛋白质折叠状态的信息传递到细胞核和胞质溶胶,以调整细胞的蛋白质折叠能力,或者在发生慢性损伤的情况下,诱导凋亡细胞死亡。在理解 UPR 信号调节及其在疾病病理生理学中的意义方面的最新进展可能会开辟新的治疗途径。

更新日期:2020-05-26
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