About this Research Topic
In nature, plants are routinely exposed to the adverse environmental conditions, which negatively affect plants growth and development by inducing protein misfolding, denaturation, oxidation and aggregation. Since the accumulation of dysfunctional proteins cause cellular toxicity, mechanisms that can effectively prevent of proteins from damage and efficiently degrade damaged proteins, are essential for plant survival under adverse environmental conditions.
Through evolution, plants have developed a comprehensive protein quality controlling system that maintains protein homeostasis, including heat shock proteins (HSPs), unfolded protein response (UPR), ubiquitin–proteasome system and autophagy. Under individual or combined environmental stresses, HSPs are abundantly synthesized to prevent proteins misfolding and aggregation as chaperones, while the accumulation of misfolded proteins in endoplasmic reticulum (ER) activates UPR to promote protein folding and degrade the mRNA of encoding proteins. When the demand exceeds the capacity of plant cells for protein repair or folding, the protein degradation systems are elicited, mainly including ubiquitin–proteasome system and autophagy. In the ubiquitin–proteasome system, after being tagged with ubiquitin, misfolded proteins in ER are transported to 26S proteasome for degradation, which is also called ER-associated protein degradation system (ERAD). In autophagy system, after being enveloped in double-membrane autophagosomes, misfolded proteins are delivered to the vacuole for breakdown and recycling.
With the unprecedented global warming, the occurrence of extreme weather is becoming more frequent, which has a negative effect on plant growth and crop production, especially in the low latitude regions. A better understanding of the mechanisms of plant tolerant to environmental stresses may provide valuable clues to crop breeders for enhancing crop productivity in the face of climate change. Since under unfavorable environments, the timely activation and cooperation of protein processing systems are vital for maintaining a proper proteostasis, this Research Topic aims to cover the identification, functional analysis, signaling, transcriptional regulation, protein modification and interaction of candidate components in all protein processing systems. We welcome all types of articles (original research, method, opinion and review) that provide new insights into our understanding of protein quality control systems in plants adaptation to environmental stresses.
Through evolution, plants have developed a comprehensive protein quality controlling system that maintains protein homeostasis, including heat shock proteins (HSPs), unfolded protein response (UPR), ubiquitin–proteasome system and autophagy. Under individual or combined environmental stresses, HSPs are abundantly synthesized to prevent proteins misfolding and aggregation as chaperones, while the accumulation of misfolded proteins in endoplasmic reticulum (ER) activates UPR to promote protein folding and degrade the mRNA of encoding proteins. When the demand exceeds the capacity of plant cells for protein repair or folding, the protein degradation systems are elicited, mainly including ubiquitin–proteasome system and autophagy. In the ubiquitin–proteasome system, after being tagged with ubiquitin, misfolded proteins in ER are transported to 26S proteasome for degradation, which is also called ER-associated protein degradation system (ERAD). In autophagy system, after being enveloped in double-membrane autophagosomes, misfolded proteins are delivered to the vacuole for breakdown and recycling.
With the unprecedented global warming, the occurrence of extreme weather is becoming more frequent, which has a negative effect on plant growth and crop production, especially in the low latitude regions. A better understanding of the mechanisms of plant tolerant to environmental stresses may provide valuable clues to crop breeders for enhancing crop productivity in the face of climate change. Since under unfavorable environments, the timely activation and cooperation of protein processing systems are vital for maintaining a proper proteostasis, this Research Topic aims to cover the identification, functional analysis, signaling, transcriptional regulation, protein modification and interaction of candidate components in all protein processing systems. We welcome all types of articles (original research, method, opinion and review) that provide new insights into our understanding of protein quality control systems in plants adaptation to environmental stresses.
Keywords: plant, heat shcok proteins, unfolded protein response, proteasome, autophagy, abiotic stress
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