(De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants
The increasing dynamic functions of post-translational modifications (PTMs) within protein molecules present outstanding challenges for plant biology even at this present day. Protein PTMs are among the first and fastest plant responses to changes in the environment, indicating that the mechanism...
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Language: | English |
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2022
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Online Access: | https://doi.org/ 10.3390/life12020324 http://hdl.handle.net/11408/5038 |
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author | Muleya, Victor Lois, L. Maria Chahtane, Hicham Thomas, Ludivine Chiapello, Marco Marondedze, Claudius |
author_facet | Muleya, Victor Lois, L. Maria Chahtane, Hicham Thomas, Ludivine Chiapello, Marco Marondedze, Claudius |
author_sort | Muleya, Victor |
collection | DSpace |
description | The increasing dynamic functions of post-translational modifications (PTMs) within protein
molecules present outstanding challenges for plant biology even at this present day. Protein PTMs
are among the first and fastest plant responses to changes in the environment, indicating that the
mechanisms and dynamics of PTMs are an essential area of plant biology. Besides being key players
in signaling, PTMs play vital roles in gene expression, gene, and protein localization, protein stability
and interactions, as well as enzyme kinetics. In this review, we take a broader but concise approach
to capture the current state of events in the field of plant PTMs. We discuss protein modifications
including citrullination, glycosylation, phosphorylation, oxidation and disulfide bridges, N-terminal,
SUMOylation, and ubiquitination. Further, we outline the complexity of studying PTMs in relation
to compartmentalization and function. We conclude by challenging the proteomics community to
engage in holistic approaches towards identification and characterizing multiple PTMs on the same
protein, their interaction, and mechanism of regulation to bring a deeper understanding of protein
function and regulation in plants. |
format | Article |
id | ir-11408-5038 |
institution | My University |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | dspace |
spelling | ir-11408-50382022-10-15T20:04:50Z (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants Muleya, Victor Lois, L. Maria Chahtane, Hicham Thomas, Ludivine Chiapello, Marco Marondedze, Claudius plant post-translational modifications phosphorylation N-glycosylation methionine oxidation N-terminal acetylation The increasing dynamic functions of post-translational modifications (PTMs) within protein molecules present outstanding challenges for plant biology even at this present day. Protein PTMs are among the first and fastest plant responses to changes in the environment, indicating that the mechanisms and dynamics of PTMs are an essential area of plant biology. Besides being key players in signaling, PTMs play vital roles in gene expression, gene, and protein localization, protein stability and interactions, as well as enzyme kinetics. In this review, we take a broader but concise approach to capture the current state of events in the field of plant PTMs. We discuss protein modifications including citrullination, glycosylation, phosphorylation, oxidation and disulfide bridges, N-terminal, SUMOylation, and ubiquitination. Further, we outline the complexity of studying PTMs in relation to compartmentalization and function. We conclude by challenging the proteomics community to engage in holistic approaches towards identification and characterizing multiple PTMs on the same protein, their interaction, and mechanism of regulation to bring a deeper understanding of protein function and regulation in plants. 2022-08-02T18:34:43Z 2022-08-02T18:34:43Z 2022-02-21 Article Muleya, V.; Lois, L.M.; Chahtane, H.; Thomas, L.; Chiapello, M.; Marondedze, C. (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants. Life 2022, 12, 324. https://doi.org/ 10.3390/life12020324 2075-1729 https://doi.org/ 10.3390/life12020324 http://hdl.handle.net/11408/5038 en Life;Vol. 12, Issue 2, No. 324. open MDPI |
spellingShingle | plant post-translational modifications phosphorylation N-glycosylation methionine oxidation N-terminal acetylation Muleya, Victor Lois, L. Maria Chahtane, Hicham Thomas, Ludivine Chiapello, Marco Marondedze, Claudius (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants |
title | (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants |
title_full | (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants |
title_fullStr | (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants |
title_full_unstemmed | (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants |
title_short | (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants |
title_sort | (de)activation (ir)reversibly or degradation: dynamics of post-translational protein modifications in plants |
topic | plant post-translational modifications phosphorylation N-glycosylation methionine oxidation N-terminal acetylation |
url | https://doi.org/ 10.3390/life12020324 http://hdl.handle.net/11408/5038 |
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