Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana

Systemic acquired resistance (SAR) in plants is a defense response that provides resistance against a wide range of pathogens at the whole-plant level following primary infection. Although the molecular mechanisms of SAR have been extensively studied in recent years, the role of phosphorylation that...

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Autores principales:	Qingfeng Zhou, Qi Meng, Xiaomin Tan, Wei Ding, Kang Ma, Ziqin Xu, Xuan Huang, Hang Gao
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	phosphoproteomics Arabidopsis systemic acquired resistance data-independent acquisition calcium-dependent protein kinase (CDPK) MAPK Plant culture SB1-1110
Acceso en línea:	https://doaj.org/article/aee84fc5dc954e759527daa33c19ac9e
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spelling	oai:doaj.org-article:aee84fc5dc954e759527daa33c19ac9e2021-11-11T10:17:06ZProtein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana1664-462X10.3389/fpls.2021.748287https://doaj.org/article/aee84fc5dc954e759527daa33c19ac9e2021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fpls.2021.748287/fullhttps://doaj.org/toc/1664-462XSystemic acquired resistance (SAR) in plants is a defense response that provides resistance against a wide range of pathogens at the whole-plant level following primary infection. Although the molecular mechanisms of SAR have been extensively studied in recent years, the role of phosphorylation that occurs in systemic leaves of SAR-induced plants is poorly understood. We used a data-independent acquisition (DIA) phosphoproteomics platform based on high-resolution mass spectrometry in an Arabidopsis thaliana model to identify phosphoproteins related to SAR establishment. A total of 8011 phosphorylation sites from 3234 proteins were identified in systemic leaves of Pseudomonas syringae pv. maculicola ES4326 (Psm ES4326) and mock locally inoculated plants. A total of 859 significantly changed phosphoproteins from 1119 significantly changed phosphopeptides were detected in systemic leaves of Psm ES4326 locally inoculated plants, including numerous transcription factors and kinases. A variety of defense response-related proteins were found to be differentially phosphorylated in systemic leaves of Psm ES4326 locally inoculated leaves, suggesting that these proteins may be functionally involved in SAR through phosphorylation or dephosphorylation. Significantly changed phosphoproteins were enriched mainly in categories related to response to abscisic acid, regulation of stomatal movement, plant–pathogen interaction, MAPK signaling pathway, purine metabolism, photosynthesis-antenna proteins, and flavonoid biosynthesis. A total of 28 proteins were regulated at both protein and phosphorylation levels during SAR. RT-qPCR analysis revealed that changes in phosphorylation levels of proteins during SAR did not result from changes in transcript abundance. This study provides comprehensive details of key phosphoproteins associated with SAR, which will facilitate further research on the molecular mechanisms of SAR.Qingfeng ZhouQi MengXiaomin TanWei DingKang MaZiqin XuXuan HuangHang GaoFrontiers Media S.A.articlephosphoproteomicsArabidopsissystemic acquired resistancedata-independent acquisitioncalcium-dependent protein kinase (CDPK)MAPKPlant cultureSB1-1110ENFrontiers in Plant Science, Vol 12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	phosphoproteomics Arabidopsis systemic acquired resistance data-independent acquisition calcium-dependent protein kinase (CDPK) MAPK Plant culture SB1-1110
spellingShingle	phosphoproteomics Arabidopsis systemic acquired resistance data-independent acquisition calcium-dependent protein kinase (CDPK) MAPK Plant culture SB1-1110 Qingfeng Zhou Qi Meng Xiaomin Tan Wei Ding Kang Ma Ziqin Xu Xuan Huang Hang Gao Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
description	Systemic acquired resistance (SAR) in plants is a defense response that provides resistance against a wide range of pathogens at the whole-plant level following primary infection. Although the molecular mechanisms of SAR have been extensively studied in recent years, the role of phosphorylation that occurs in systemic leaves of SAR-induced plants is poorly understood. We used a data-independent acquisition (DIA) phosphoproteomics platform based on high-resolution mass spectrometry in an Arabidopsis thaliana model to identify phosphoproteins related to SAR establishment. A total of 8011 phosphorylation sites from 3234 proteins were identified in systemic leaves of Pseudomonas syringae pv. maculicola ES4326 (Psm ES4326) and mock locally inoculated plants. A total of 859 significantly changed phosphoproteins from 1119 significantly changed phosphopeptides were detected in systemic leaves of Psm ES4326 locally inoculated plants, including numerous transcription factors and kinases. A variety of defense response-related proteins were found to be differentially phosphorylated in systemic leaves of Psm ES4326 locally inoculated leaves, suggesting that these proteins may be functionally involved in SAR through phosphorylation or dephosphorylation. Significantly changed phosphoproteins were enriched mainly in categories related to response to abscisic acid, regulation of stomatal movement, plant–pathogen interaction, MAPK signaling pathway, purine metabolism, photosynthesis-antenna proteins, and flavonoid biosynthesis. A total of 28 proteins were regulated at both protein and phosphorylation levels during SAR. RT-qPCR analysis revealed that changes in phosphorylation levels of proteins during SAR did not result from changes in transcript abundance. This study provides comprehensive details of key phosphoproteins associated with SAR, which will facilitate further research on the molecular mechanisms of SAR.
format	article
author	Qingfeng Zhou Qi Meng Xiaomin Tan Wei Ding Kang Ma Ziqin Xu Xuan Huang Hang Gao
author_facet	Qingfeng Zhou Qi Meng Xiaomin Tan Wei Ding Kang Ma Ziqin Xu Xuan Huang Hang Gao
author_sort	Qingfeng Zhou
title	Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_short	Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_full	Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_fullStr	Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_full_unstemmed	Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_sort	protein phosphorylation changes during systemic acquired resistance in arabidopsis thaliana
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/aee84fc5dc954e759527daa33c19ac9e
work_keys_str_mv	AT qingfengzhou proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana AT qimeng proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana AT xiaomintan proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana AT weiding proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana AT kangma proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana AT ziqinxu proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana AT xuanhuang proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana AT hanggao proteinphosphorylationchangesduringsystemicacquiredresistanceinarabidopsisthaliana
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Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana

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