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How Many Faces Does the Plant U-Box E3 Ligase Have?
Ubiquitination is a major type of post-translational modification of proteins in eukaryotes. The plant U-Box (PUB) E3 ligase is the smallest family in the E3 ligase superfamily, but plays a variety of essential roles in plant growth, development and response to diverse environmental stresses. Hence,...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8875423/ https://www.ncbi.nlm.nih.gov/pubmed/35216399 http://dx.doi.org/10.3390/ijms23042285 |
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author | Mao, Xinguo Yu, Chunmei Li, Long Wang, Min Yang, Lili Zhang, Yining Zhang, Yanfei Wang, Jingyi Li, Chaonan Reynolds, Matthew Paul Jing, Ruilian |
author_facet | Mao, Xinguo Yu, Chunmei Li, Long Wang, Min Yang, Lili Zhang, Yining Zhang, Yanfei Wang, Jingyi Li, Chaonan Reynolds, Matthew Paul Jing, Ruilian |
author_sort | Mao, Xinguo |
collection | PubMed |
description | Ubiquitination is a major type of post-translational modification of proteins in eukaryotes. The plant U-Box (PUB) E3 ligase is the smallest family in the E3 ligase superfamily, but plays a variety of essential roles in plant growth, development and response to diverse environmental stresses. Hence, PUBs are potential gene resources for developing climate-resilient crops. However, there is a lack of review of the latest advances to fully understand the powerful gene family. To bridge the gap and facilitate its use in future crop breeding, we comprehensively summarize the recent progress of the PUB family, including gene evolution, classification, biological functions, and multifarious regulatory mechanisms in plants. |
format | Online Article Text |
id | pubmed-8875423 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88754232022-02-26 How Many Faces Does the Plant U-Box E3 Ligase Have? Mao, Xinguo Yu, Chunmei Li, Long Wang, Min Yang, Lili Zhang, Yining Zhang, Yanfei Wang, Jingyi Li, Chaonan Reynolds, Matthew Paul Jing, Ruilian Int J Mol Sci Review Ubiquitination is a major type of post-translational modification of proteins in eukaryotes. The plant U-Box (PUB) E3 ligase is the smallest family in the E3 ligase superfamily, but plays a variety of essential roles in plant growth, development and response to diverse environmental stresses. Hence, PUBs are potential gene resources for developing climate-resilient crops. However, there is a lack of review of the latest advances to fully understand the powerful gene family. To bridge the gap and facilitate its use in future crop breeding, we comprehensively summarize the recent progress of the PUB family, including gene evolution, classification, biological functions, and multifarious regulatory mechanisms in plants. MDPI 2022-02-18 /pmc/articles/PMC8875423/ /pubmed/35216399 http://dx.doi.org/10.3390/ijms23042285 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 Mao, Xinguo Yu, Chunmei Li, Long Wang, Min Yang, Lili Zhang, Yining Zhang, Yanfei Wang, Jingyi Li, Chaonan Reynolds, Matthew Paul Jing, Ruilian How Many Faces Does the Plant U-Box E3 Ligase Have? |
title | How Many Faces Does the Plant U-Box E3 Ligase Have? |
title_full | How Many Faces Does the Plant U-Box E3 Ligase Have? |
title_fullStr | How Many Faces Does the Plant U-Box E3 Ligase Have? |
title_full_unstemmed | How Many Faces Does the Plant U-Box E3 Ligase Have? |
title_short | How Many Faces Does the Plant U-Box E3 Ligase Have? |
title_sort | how many faces does the plant u-box e3 ligase have? |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8875423/ https://www.ncbi.nlm.nih.gov/pubmed/35216399 http://dx.doi.org/10.3390/ijms23042285 |
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