Quantitative Phosphoproteomics of cipk3/9/23/26 Mutant and Wild Type in Arabidopsis thaliana

CBL-interacting protein kinases 3/9/23/26 (CIPK3/9/23/26) are central regulation components of magnesium ion homeostasis. CBL2/3 interacts with CIPK3/9/23/26, which phosphorylates their downstream targets, suggesting that protein phosphorylation is a key factor influencing the maintenance of cellula...

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Autores principales:	Ziyi Yin, Jisen Shi, Yan Zhen
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	<i>Arabidopsis thaliana</i> L. CBL-interacting protein kinases 6 signal transduction magnesium sensitivity tandem mass tag labeling Genetics QH426-470
Acceso en línea:	https://doaj.org/article/74fde0ad91f34f04981e944d91a1eb7c
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spelling	oai:doaj.org-article:74fde0ad91f34f04981e944d91a1eb7c2021-11-25T17:41:36ZQuantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>10.3390/genes121117592073-4425https://doaj.org/article/74fde0ad91f34f04981e944d91a1eb7c2021-11-01T00:00:00Zhttps://www.mdpi.com/2073-4425/12/11/1759https://doaj.org/toc/2073-4425CBL-interacting protein kinases 3/9/23/26 (CIPK3/9/23/26) are central regulation components of magnesium ion homeostasis. CBL2/3 interacts with CIPK3/9/23/26, which phosphorylates their downstream targets, suggesting that protein phosphorylation is a key factor influencing the maintenance of cellular magnesium homeostasis in higher plants. The <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> quadruple mutant is very sensitive to high levels of magnesium. In this study, TMT quantitative phosphoproteomics were used to compare the global variations in phosphoproteins in wild type and <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> quadruple mutant seedlings of <i>Arabidopsis thaliana</i>, and 12,506 phosphorylation modification sites on 4537 proteins were identified, of which 773 phosphorylated proteins exhibited significant variations at the phosphorylation level under magnesium sensitivity. Subsequently, we used bioinformatics methods to systematically annotate and analyze the data. Certain transporters and signaling components that could be associated with magnesium sensitivity, such as ATP-binding cassette transporters and mitogen-activated protein kinases, were identified. The results of this study further our understanding of the molecular mechanisms of CIPK3/9/23/26 in mediating magnesium homeostasis.Ziyi YinJisen ShiYan ZhenMDPI AGarticle<i>Arabidopsis thaliana</i> L.CBL-interacting protein kinases 6signal transductionmagnesium sensitivitytandem mass tag labelingGeneticsQH426-470ENGenes, Vol 12, Iss 1759, p 1759 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	<i>Arabidopsis thaliana</i> L. CBL-interacting protein kinases 6 signal transduction magnesium sensitivity tandem mass tag labeling Genetics QH426-470
spellingShingle	<i>Arabidopsis thaliana</i> L. CBL-interacting protein kinases 6 signal transduction magnesium sensitivity tandem mass tag labeling Genetics QH426-470 Ziyi Yin Jisen Shi Yan Zhen Quantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>
description	CBL-interacting protein kinases 3/9/23/26 (CIPK3/9/23/26) are central regulation components of magnesium ion homeostasis. CBL2/3 interacts with CIPK3/9/23/26, which phosphorylates their downstream targets, suggesting that protein phosphorylation is a key factor influencing the maintenance of cellular magnesium homeostasis in higher plants. The <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> quadruple mutant is very sensitive to high levels of magnesium. In this study, TMT quantitative phosphoproteomics were used to compare the global variations in phosphoproteins in wild type and <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> quadruple mutant seedlings of <i>Arabidopsis thaliana</i>, and 12,506 phosphorylation modification sites on 4537 proteins were identified, of which 773 phosphorylated proteins exhibited significant variations at the phosphorylation level under magnesium sensitivity. Subsequently, we used bioinformatics methods to systematically annotate and analyze the data. Certain transporters and signaling components that could be associated with magnesium sensitivity, such as ATP-binding cassette transporters and mitogen-activated protein kinases, were identified. The results of this study further our understanding of the molecular mechanisms of CIPK3/9/23/26 in mediating magnesium homeostasis.
format	article
author	Ziyi Yin Jisen Shi Yan Zhen
author_facet	Ziyi Yin Jisen Shi Yan Zhen
author_sort	Ziyi Yin
title	Quantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>
title_short	Quantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>
title_full	Quantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>
title_fullStr	Quantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>
title_full_unstemmed	Quantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>
title_sort	quantitative phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> mutant and wild type in <i>arabidopsis thaliana</i>
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/74fde0ad91f34f04981e944d91a1eb7c
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_version_	1718412111408791552

Quantitative Phosphoproteomics of <i>cipk3</i>/<i>9</i>/<i>23</i>/<i>26</i> Mutant and Wild Type in <i>Arabidopsis thaliana</i>

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