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Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses

Plants are frequently exposed to a variety of abiotic stresses, such as those caused by salt, drought, cold, and heat. All of these stressors can induce changes in the proteoforms, which make up the proteome of an organism. Of the many different proteoforms, protein ubiquitination has attracted a lo...

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Autores principales: Wang, Shuang, Lv, Xiaoyan, Zhang, Jialin, Chen, Daniel, Chen, Sixue, Fan, Guoquan, Ma, Chunquan, Wang, Yuguang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8878164/
https://www.ncbi.nlm.nih.gov/pubmed/35216424
http://dx.doi.org/10.3390/ijms23042308
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author Wang, Shuang
Lv, Xiaoyan
Zhang, Jialin
Chen, Daniel
Chen, Sixue
Fan, Guoquan
Ma, Chunquan
Wang, Yuguang
author_facet Wang, Shuang
Lv, Xiaoyan
Zhang, Jialin
Chen, Daniel
Chen, Sixue
Fan, Guoquan
Ma, Chunquan
Wang, Yuguang
author_sort Wang, Shuang
collection PubMed
description Plants are frequently exposed to a variety of abiotic stresses, such as those caused by salt, drought, cold, and heat. All of these stressors can induce changes in the proteoforms, which make up the proteome of an organism. Of the many different proteoforms, protein ubiquitination has attracted a lot of attention because it is widely involved in the process of protein degradation; thus regulates many plants molecular processes, such as hormone signal transduction, to resist external stresses. Ubiquitin ligases are crucial in substrate recognition during this ubiquitin modification process. In this review, the molecular mechanisms of plant responses to abiotic stresses from the perspective of ubiquitin ligases have been described. This information is critical for a better understanding of plant molecular responses to abiotic stresses.
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spelling pubmed-88781642022-02-26 Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses Wang, Shuang Lv, Xiaoyan Zhang, Jialin Chen, Daniel Chen, Sixue Fan, Guoquan Ma, Chunquan Wang, Yuguang Int J Mol Sci Review Plants are frequently exposed to a variety of abiotic stresses, such as those caused by salt, drought, cold, and heat. All of these stressors can induce changes in the proteoforms, which make up the proteome of an organism. Of the many different proteoforms, protein ubiquitination has attracted a lot of attention because it is widely involved in the process of protein degradation; thus regulates many plants molecular processes, such as hormone signal transduction, to resist external stresses. Ubiquitin ligases are crucial in substrate recognition during this ubiquitin modification process. In this review, the molecular mechanisms of plant responses to abiotic stresses from the perspective of ubiquitin ligases have been described. This information is critical for a better understanding of plant molecular responses to abiotic stresses. MDPI 2022-02-19 /pmc/articles/PMC8878164/ /pubmed/35216424 http://dx.doi.org/10.3390/ijms23042308 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Wang, Shuang
Lv, Xiaoyan
Zhang, Jialin
Chen, Daniel
Chen, Sixue
Fan, Guoquan
Ma, Chunquan
Wang, Yuguang
Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
title Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
title_full Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
title_fullStr Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
title_full_unstemmed Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
title_short Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
title_sort roles of e3 ubiquitin ligases in plant responses to abiotic stresses
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8878164/
https://www.ncbi.nlm.nih.gov/pubmed/35216424
http://dx.doi.org/10.3390/ijms23042308
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