未折叠蛋白反应
内质网
细胞生物学
内质网相关蛋白降解
伴侣(临床)
蛋白质折叠
分泌途径
生物
高尔基体
医学
病理
作者
Wahyu Indra Duwi Fanata,Sang Yeol Lee,Kyun Oh Lee
标识
DOI:10.1016/j.jprot.2013.04.023
摘要
In eukaryotic cells, proteins that enter the secretory pathway are translated on membrane-bound ribosomes and translocated into the endoplasmic reticulum (ER), where they are subjected to chaperone-assisted folding, post-translational modification and assembly. During the evolution of the eukaryotic cell, a homeostatic mechanism was developed to maintain the functions of the ER in the face of various internal and external stresses. The most severe stresses imposed on eukaryotic cells can induce ER stress that can overwhelm the processing capacity of the ER, leading to the accumulation of unfolded proteins in the ER lumen. To cope with this accumulation of unfolded proteins, the unfolded protein response (UPR) is activated to alter transcriptional programs through inositol-requiring enzyme 1 (IRE1) and bZIP17/28 in plants. In addition to transcriptional induction of UPR genes, quality control (QC), translational attenuation, ER-associated degradation (ERAD) and ER stress-induced apoptosis are also conserved as fundamental adaptive cellular responses to ER stress in plants. This article is part of a Special Issue entitled: Translational Plant Proteomics.
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