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Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana

Although arsenite [As(III)] is non-essential and toxic for plants, it is effectively absorbed through various transporters into the roots. Here we identified a calcium-dependent protein kinase (CPK31) response for As(III) tolerance in Arabidopsis. We identified CPK31 as an interacting protein of a n...

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Autores principales: Ji, Ruijie, Zhou, Liming, Liu, Jinglong, Wang, Yuan, Yang, Lei, Zheng, Qinsong, Zhang, Chi, Zhang, Bin, Ge, Haiman, Yang, Yonghua, Zhao, Fugeng, Luan, Sheng, Lan, Wenzhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5351991/
https://www.ncbi.nlm.nih.gov/pubmed/28296918
http://dx.doi.org/10.1371/journal.pone.0173681
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author Ji, Ruijie
Zhou, Liming
Liu, Jinglong
Wang, Yuan
Yang, Lei
Zheng, Qinsong
Zhang, Chi
Zhang, Bin
Ge, Haiman
Yang, Yonghua
Zhao, Fugeng
Luan, Sheng
Lan, Wenzhi
author_facet Ji, Ruijie
Zhou, Liming
Liu, Jinglong
Wang, Yuan
Yang, Lei
Zheng, Qinsong
Zhang, Chi
Zhang, Bin
Ge, Haiman
Yang, Yonghua
Zhao, Fugeng
Luan, Sheng
Lan, Wenzhi
author_sort Ji, Ruijie
collection PubMed
description Although arsenite [As(III)] is non-essential and toxic for plants, it is effectively absorbed through various transporters into the roots. Here we identified a calcium-dependent protein kinase (CPK31) response for As(III) tolerance in Arabidopsis. We identified CPK31 as an interacting protein of a nodulin 26-like intrinsic protein (NIP1;1), an aquaporin involved in As(III) uptake. Similarly to the nip1;1 mutants, the loss-of-function mutants of CPK31 improved the tolerance against As(III) but not As(V), and accumulated less As(III) in roots than that of the wild-type plants. The promoter-β-glucuronidase and quantitative Real-Time PCR analysis revealed that CPK31 displayed overlapping expression profiles with NIP1;1 in the roots, suggesting that they might function together in roots. Indeed, the cpk31 nip1;1 double mutants exhibited stronger As(III) tolerance than cpk31 mutants, but similar to nip1;1 mutants, supporting the idea that CPK31 might serve as an upstream regulator of NIP1;1. Furthermore, transient CPK31 overexpression induced by dexamethasone caused the decrease in As(III) tolerance of transgenic Arabidopsis lines. These findings reveal that CPK31 is a key factor in As(III) response in plants.
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spelling pubmed-53519912017-04-06 Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana Ji, Ruijie Zhou, Liming Liu, Jinglong Wang, Yuan Yang, Lei Zheng, Qinsong Zhang, Chi Zhang, Bin Ge, Haiman Yang, Yonghua Zhao, Fugeng Luan, Sheng Lan, Wenzhi PLoS One Research Article Although arsenite [As(III)] is non-essential and toxic for plants, it is effectively absorbed through various transporters into the roots. Here we identified a calcium-dependent protein kinase (CPK31) response for As(III) tolerance in Arabidopsis. We identified CPK31 as an interacting protein of a nodulin 26-like intrinsic protein (NIP1;1), an aquaporin involved in As(III) uptake. Similarly to the nip1;1 mutants, the loss-of-function mutants of CPK31 improved the tolerance against As(III) but not As(V), and accumulated less As(III) in roots than that of the wild-type plants. The promoter-β-glucuronidase and quantitative Real-Time PCR analysis revealed that CPK31 displayed overlapping expression profiles with NIP1;1 in the roots, suggesting that they might function together in roots. Indeed, the cpk31 nip1;1 double mutants exhibited stronger As(III) tolerance than cpk31 mutants, but similar to nip1;1 mutants, supporting the idea that CPK31 might serve as an upstream regulator of NIP1;1. Furthermore, transient CPK31 overexpression induced by dexamethasone caused the decrease in As(III) tolerance of transgenic Arabidopsis lines. These findings reveal that CPK31 is a key factor in As(III) response in plants. Public Library of Science 2017-03-15 /pmc/articles/PMC5351991/ /pubmed/28296918 http://dx.doi.org/10.1371/journal.pone.0173681 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 (https://creativecommons.org/publicdomain/zero/1.0/) public domain dedication.
spellingShingle Research Article
Ji, Ruijie
Zhou, Liming
Liu, Jinglong
Wang, Yuan
Yang, Lei
Zheng, Qinsong
Zhang, Chi
Zhang, Bin
Ge, Haiman
Yang, Yonghua
Zhao, Fugeng
Luan, Sheng
Lan, Wenzhi
Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana
title Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana
title_full Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana
title_fullStr Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana
title_full_unstemmed Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana
title_short Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana
title_sort calcium-dependent protein kinase cpk31 interacts with arsenic transporter atnip1;1 and regulates arsenite uptake in arabidopsis thaliana
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5351991/
https://www.ncbi.nlm.nih.gov/pubmed/28296918
http://dx.doi.org/10.1371/journal.pone.0173681
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