Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia

Abstract Background Senescence represents the last stage of flower development. Phosphorylation is the key posttranslational modification that regulates protein functions, and kinases may be more required than phosphatases during plant growth and development. However, little is known about global ph...

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Autores principales:	Shiwei Zhong, Lina Sang, Zhixia Zhao, Ying Deng, Haitao Liu, Yixun Yu, Juanxu Liu
Formato:	article
Lenguaje:	EN
Publicado:	BMC 2021
Materias:	Ethylene Phosphorylation Senescence Petunia Dephosphorylation Alternative splicing Botany QK1-989
Acceso en línea:	https://doaj.org/article/50b1bc7eef924e969dcec19e9fd88876
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spelling	oai:doaj.org-article:50b1bc7eef924e969dcec19e9fd888762021-11-07T12:09:17ZPhosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia10.1186/s12870-021-03286-x1471-2229https://doaj.org/article/50b1bc7eef924e969dcec19e9fd888762021-11-01T00:00:00Zhttps://doi.org/10.1186/s12870-021-03286-xhttps://doaj.org/toc/1471-2229Abstract Background Senescence represents the last stage of flower development. Phosphorylation is the key posttranslational modification that regulates protein functions, and kinases may be more required than phosphatases during plant growth and development. However, little is known about global phosphorylation changes during flower senescence. Results In this work, we quantitatively investigated the petunia phosphoproteome following ethylene or air treatment. In total, 2170 phosphosites in 1184 protein groups were identified, among which 2059 sites in 1124 proteins were quantified. To our surprise, treatment with ethylene resulted in 697 downregulated and only 117 upregulated phosphosites using a 1.5-fold threshold (FDR < 0.05), which showed that ethylene negatively regulates global phosphorylation levels and that phosphorylation of many proteins was not necessary during flower senescence. Phosphoproteome analysis showed that ethylene regulates ethylene and ABA signalling transduction pathways via phosphorylation levels. One of the major targets of ethylene-induced dephosphorylation is the plant mRNA splicing machinery, and ethylene treatment increases the number of alternative splicing events of precursor RNAs in petunia corollas. Conclusions Protein dephosphorylation could play an important role in ethylene-induced senescence, and ethylene treatment increased the number of AS precursor RNAs in petunia corollas.Shiwei ZhongLina SangZhixia ZhaoYing DengHaitao LiuYixun YuJuanxu LiuBMCarticleEthylenePhosphorylationSenescencePetuniaDephosphorylationAlternative splicingBotanyQK1-989ENBMC Plant Biology, Vol 21, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Ethylene Phosphorylation Senescence Petunia Dephosphorylation Alternative splicing Botany QK1-989
spellingShingle	Ethylene Phosphorylation Senescence Petunia Dephosphorylation Alternative splicing Botany QK1-989 Shiwei Zhong Lina Sang Zhixia Zhao Ying Deng Haitao Liu Yixun Yu Juanxu Liu Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia
description	Abstract Background Senescence represents the last stage of flower development. Phosphorylation is the key posttranslational modification that regulates protein functions, and kinases may be more required than phosphatases during plant growth and development. However, little is known about global phosphorylation changes during flower senescence. Results In this work, we quantitatively investigated the petunia phosphoproteome following ethylene or air treatment. In total, 2170 phosphosites in 1184 protein groups were identified, among which 2059 sites in 1124 proteins were quantified. To our surprise, treatment with ethylene resulted in 697 downregulated and only 117 upregulated phosphosites using a 1.5-fold threshold (FDR < 0.05), which showed that ethylene negatively regulates global phosphorylation levels and that phosphorylation of many proteins was not necessary during flower senescence. Phosphoproteome analysis showed that ethylene regulates ethylene and ABA signalling transduction pathways via phosphorylation levels. One of the major targets of ethylene-induced dephosphorylation is the plant mRNA splicing machinery, and ethylene treatment increases the number of alternative splicing events of precursor RNAs in petunia corollas. Conclusions Protein dephosphorylation could play an important role in ethylene-induced senescence, and ethylene treatment increased the number of AS precursor RNAs in petunia corollas.
format	article
author	Shiwei Zhong Lina Sang Zhixia Zhao Ying Deng Haitao Liu Yixun Yu Juanxu Liu
author_facet	Shiwei Zhong Lina Sang Zhixia Zhao Ying Deng Haitao Liu Yixun Yu Juanxu Liu
author_sort	Shiwei Zhong
title	Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia
title_short	Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia
title_full	Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia
title_fullStr	Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia
title_full_unstemmed	Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia
title_sort	phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia
publisher	BMC
publishDate	2021
url	https://doaj.org/article/50b1bc7eef924e969dcec19e9fd88876
work_keys_str_mv	AT shiweizhong phosphoproteomeanalysisrevealstheinvolvementofproteindephosphorylationinethyleneinducedcorollasenescenceinpetunia AT linasang phosphoproteomeanalysisrevealstheinvolvementofproteindephosphorylationinethyleneinducedcorollasenescenceinpetunia AT zhixiazhao phosphoproteomeanalysisrevealstheinvolvementofproteindephosphorylationinethyleneinducedcorollasenescenceinpetunia AT yingdeng phosphoproteomeanalysisrevealstheinvolvementofproteindephosphorylationinethyleneinducedcorollasenescenceinpetunia AT haitaoliu phosphoproteomeanalysisrevealstheinvolvementofproteindephosphorylationinethyleneinducedcorollasenescenceinpetunia AT yixunyu phosphoproteomeanalysisrevealstheinvolvementofproteindephosphorylationinethyleneinducedcorollasenescenceinpetunia AT juanxuliu phosphoproteomeanalysisrevealstheinvolvementofproteindephosphorylationinethyleneinducedcorollasenescenceinpetunia
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Phosphoproteome analysis reveals the involvement of protein dephosphorylation in ethylene-induced corolla senescence in petunia

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