Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 14, Issue 4, Pages 8188-8212Publisher
MDPI
DOI: 10.3390/ijms14048188
Keywords
endoplasmic reticulum stress; unfolded protein response (UPR); endoplasmic reticulum quality control (ERQC); endoplasmic reticulum associated degradation (ERAD); autophagy; cell death
Funding
- National Science Foundation [IOS90917]
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [0919707] Funding Source: National Science Foundation
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The endoplasmic reticulum (ER) stress response is a highly conserved mechanism that results from the accumulation of unfolded or misfolded proteins in the ER. The response plays an important role in allowing plants to sense and respond to adverse environmental conditions, such as heat stress, salt stress and pathogen infection. Since the ER is a well-controlled microenvironment for proper protein synthesis and folding, it is highly susceptible to stress conditions. Accumulation of unfolded or misfolded proteins activates a signaling pathway, called the unfolded protein response (UPR), which acts to relieve ER stress and, if unsuccessful, leads to cell death. Plants have two arms of the UPR signaling pathway, an arm involving the proteolytic processing of membrane-associated basic leucine zipper domain (bZIP) transcription factors and an arm involving RNA splicing factor, IRE1, and its mRNA target. These signaling pathways play an important role in determining the cell's fate in response to stress conditions.
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