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Advances on Plant Ubiquitylome—From Mechanism to Application
Post-translational modifications (PTMs) of proteins enable modulation of their structure, function, localization and turnover. To date, over 660 PTMs have been reported, among which, reversible PTMs are regarded as the key players in cellular signaling. Signaling mediated by PTMs is faster than re-i...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7663383/ https://www.ncbi.nlm.nih.gov/pubmed/33114409 http://dx.doi.org/10.3390/ijms21217909 |
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author | He, Dongli Damaris, Rebecca Njeri Li, Ming Khan, Imran Yang, Pingfang |
author_facet | He, Dongli Damaris, Rebecca Njeri Li, Ming Khan, Imran Yang, Pingfang |
author_sort | He, Dongli |
collection | PubMed |
description | Post-translational modifications (PTMs) of proteins enable modulation of their structure, function, localization and turnover. To date, over 660 PTMs have been reported, among which, reversible PTMs are regarded as the key players in cellular signaling. Signaling mediated by PTMs is faster than re-initiation of gene expression, which may result in a faster response that is particularly crucial for plants due to their sessile nature. Ubiquitylation has been widely reported to be involved in many aspects of plant growth and development and it is largely determined by its target protein. It is therefore of high interest to explore new ubiquitylated proteins/sites to obtain new insights into its mechanism and functions. In the last decades, extensive protein profiling of ubiquitylation has been achieved in different plants due to the advancement in ubiquitylated proteins (or peptides) affinity and mass spectrometry techniques. This obtained information on a large number of ubiquitylated proteins/sites helps crack the mechanism of ubiquitylation in plants. In this review, we have summarized the latest advances in protein ubiquitylation to gain comprehensive and updated knowledge in this field. Besides, the current and future challenges and barriers are also reviewed and discussed. |
format | Online Article Text |
id | pubmed-7663383 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76633832020-11-14 Advances on Plant Ubiquitylome—From Mechanism to Application He, Dongli Damaris, Rebecca Njeri Li, Ming Khan, Imran Yang, Pingfang Int J Mol Sci Review Post-translational modifications (PTMs) of proteins enable modulation of their structure, function, localization and turnover. To date, over 660 PTMs have been reported, among which, reversible PTMs are regarded as the key players in cellular signaling. Signaling mediated by PTMs is faster than re-initiation of gene expression, which may result in a faster response that is particularly crucial for plants due to their sessile nature. Ubiquitylation has been widely reported to be involved in many aspects of plant growth and development and it is largely determined by its target protein. It is therefore of high interest to explore new ubiquitylated proteins/sites to obtain new insights into its mechanism and functions. In the last decades, extensive protein profiling of ubiquitylation has been achieved in different plants due to the advancement in ubiquitylated proteins (or peptides) affinity and mass spectrometry techniques. This obtained information on a large number of ubiquitylated proteins/sites helps crack the mechanism of ubiquitylation in plants. In this review, we have summarized the latest advances in protein ubiquitylation to gain comprehensive and updated knowledge in this field. Besides, the current and future challenges and barriers are also reviewed and discussed. MDPI 2020-10-24 /pmc/articles/PMC7663383/ /pubmed/33114409 http://dx.doi.org/10.3390/ijms21217909 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review He, Dongli Damaris, Rebecca Njeri Li, Ming Khan, Imran Yang, Pingfang Advances on Plant Ubiquitylome—From Mechanism to Application |
title | Advances on Plant Ubiquitylome—From Mechanism to Application |
title_full | Advances on Plant Ubiquitylome—From Mechanism to Application |
title_fullStr | Advances on Plant Ubiquitylome—From Mechanism to Application |
title_full_unstemmed | Advances on Plant Ubiquitylome—From Mechanism to Application |
title_short | Advances on Plant Ubiquitylome—From Mechanism to Application |
title_sort | advances on plant ubiquitylome—from mechanism to application |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7663383/ https://www.ncbi.nlm.nih.gov/pubmed/33114409 http://dx.doi.org/10.3390/ijms21217909 |
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