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Dealing With Stress: A Review of Plant SUMO Proteases
The SUMO system is a rapid dynamic post-translational mechanism employed by eukaryotic cells to respond to stress. Plant cells experience hyperSUMOylation of substrates in response to stresses such as heat, ethanol, and drought. Many SUMOylated proteins are located in the nucleus, SUMOylation alteri...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6759571/ https://www.ncbi.nlm.nih.gov/pubmed/31620153 http://dx.doi.org/10.3389/fpls.2019.01122 |
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author | Morrell, Rebecca Sadanandom, Ari |
author_facet | Morrell, Rebecca Sadanandom, Ari |
author_sort | Morrell, Rebecca |
collection | PubMed |
description | The SUMO system is a rapid dynamic post-translational mechanism employed by eukaryotic cells to respond to stress. Plant cells experience hyperSUMOylation of substrates in response to stresses such as heat, ethanol, and drought. Many SUMOylated proteins are located in the nucleus, SUMOylation altering many nuclear processes. The SUMO proteases play two key functions in the SUMO cycle by generating free SUMO; they have an important role in regulating the SUMO cycle, and by cleaving SUMO off SUMOylated proteins, they provide specificity to which proteins become SUMOylated. This review summarizes the broad literature of plant SUMO proteases describing their catalytic activity, domains and structure, evolution, localization, and response to stress and highlighting potential new areas of research in the future. |
format | Online Article Text |
id | pubmed-6759571 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-67595712019-10-16 Dealing With Stress: A Review of Plant SUMO Proteases Morrell, Rebecca Sadanandom, Ari Front Plant Sci Plant Science The SUMO system is a rapid dynamic post-translational mechanism employed by eukaryotic cells to respond to stress. Plant cells experience hyperSUMOylation of substrates in response to stresses such as heat, ethanol, and drought. Many SUMOylated proteins are located in the nucleus, SUMOylation altering many nuclear processes. The SUMO proteases play two key functions in the SUMO cycle by generating free SUMO; they have an important role in regulating the SUMO cycle, and by cleaving SUMO off SUMOylated proteins, they provide specificity to which proteins become SUMOylated. This review summarizes the broad literature of plant SUMO proteases describing their catalytic activity, domains and structure, evolution, localization, and response to stress and highlighting potential new areas of research in the future. Frontiers Media S.A. 2019-09-18 /pmc/articles/PMC6759571/ /pubmed/31620153 http://dx.doi.org/10.3389/fpls.2019.01122 Text en Copyright © 2019 Morrell and Sadanandom http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Morrell, Rebecca Sadanandom, Ari Dealing With Stress: A Review of Plant SUMO Proteases |
title | Dealing With Stress: A Review of Plant SUMO Proteases |
title_full | Dealing With Stress: A Review of Plant SUMO Proteases |
title_fullStr | Dealing With Stress: A Review of Plant SUMO Proteases |
title_full_unstemmed | Dealing With Stress: A Review of Plant SUMO Proteases |
title_short | Dealing With Stress: A Review of Plant SUMO Proteases |
title_sort | dealing with stress: a review of plant sumo proteases |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6759571/ https://www.ncbi.nlm.nih.gov/pubmed/31620153 http://dx.doi.org/10.3389/fpls.2019.01122 |
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