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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...

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Autores principales: He, Dongli, Damaris, Rebecca Njeri, Li, Ming, Khan, Imran, Yang, Pingfang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
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.
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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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