期刊
JOURNAL OF PROTEOMICS
卷 93, 期 -, 页码 356-368出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2013.04.023
关键词
Endoplasmic reticulum stress; Unfolded protein response; Quality control; Endoplasmic reticulum-associated; degradation; Apoptosis; Plants
资金
- Next-Generation BioGreen Program (SSAC) [PJ008109]
- Rural Development Administration
- TDPAF [609004-5]
- Ministry for Food, Agriculture, Forestry and Fisheries
- Basic Science Research Program through the National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology, Republic of Korea [2012R1A1A2001074]
- National Research Foundation of Korea [2012R1A1A2001074] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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.
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