The unfolded protein response in plants: A fundamental adaptive cellular response to internal and external stresses

被引:42
作者
Fanata, Wahyu Indra Duwi
Lee, Sang Yeol
Lee, Kyun Oh [1 ]
机构
[1] Gyeongsang Natl Univ, Div Appl Life Sci, Program BK21, Jinju 660701, South Korea
基金
新加坡国家研究基金会;
关键词
Endoplasmic reticulum stress; Unfolded protein response; Quality control; Endoplasmic reticulum-associated; degradation; Apoptosis; Plants; ENDOPLASMIC-RETICULUM STRESS; ER QUALITY-CONTROL; DEFECTIVE BRASSINOSTEROID RECEPTOR; ACTIVE TRANSCRIPTION FACTOR; GLUCOSE-REGULATED PROTEINS; MESSENGER-RNA; TRANSLATIONAL CONTROL; TRANSMEMBRANE PROTEIN; ARABIDOPSIS-THALIANA; MAMMALIAN-CELLS;
D O I
10.1016/j.jprot.2013.04.023
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
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. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:356 / 368
页数:13
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