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CARK1 mediates ABA signaling by phosphorylation of ABA receptors

The function of abscisic acid (ABA) is mediated by its receptors termed RCARs/PYR1/PYLs. Modulation of ABA signaling is vital for plant growth and development. The RCAR-PP2C-SnRK2 regulatory modules have been defined as the core components in ABA signaling. However, it is still not clear whether and...

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Autores principales: Zhang, Liang, Li, Xiaoyi, Li, Dekuan, Sun, Yuna, Li, Ying, Luo, Qin, Liu, Zhibin, Wang, Jianmei, Li, Xufeng, Zhang, Hong, Lou, Zhiyong, Yang, Yi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6006248/
https://www.ncbi.nlm.nih.gov/pubmed/29928509
http://dx.doi.org/10.1038/s41421-018-0029-y
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author Zhang, Liang
Li, Xiaoyi
Li, Dekuan
Sun, Yuna
Li, Ying
Luo, Qin
Liu, Zhibin
Wang, Jianmei
Li, Xufeng
Zhang, Hong
Lou, Zhiyong
Yang, Yi
author_facet Zhang, Liang
Li, Xiaoyi
Li, Dekuan
Sun, Yuna
Li, Ying
Luo, Qin
Liu, Zhibin
Wang, Jianmei
Li, Xufeng
Zhang, Hong
Lou, Zhiyong
Yang, Yi
author_sort Zhang, Liang
collection PubMed
description The function of abscisic acid (ABA) is mediated by its receptors termed RCARs/PYR1/PYLs. Modulation of ABA signaling is vital for plant growth and development. The RCAR-PP2C-SnRK2 regulatory modules have been defined as the core components in ABA signaling. However, it is still not clear whether and how the ABA receptors could be modified at the initial post-translational stage to fine-tune ABA transduction pathway. Here we identify and characterize the putative receptor-like cytoplasmic kinase (RLCK) in Arabidopsis named CARK1, which interacts with RCAR3 (PYL8) and RCAR11 (PYR1) in the manner of phosphorylation. Structural studies of CARK1 revealed the critical active site, N204, which accounts for the kinase activity and the direct interaction with RCAR3/RCAR11. CARK1 phosphorylates RCAR3/RCAR11 at one conserved threonine site, T77/T78. Our genetic analyses further demonstrated that CARK1 positively regulates ABA-mediated physiological responses and overexpression of CARK1 in Arabidopsis distinctly promotes the drought resistance. Moreover, the phosphor-mimic form of RCAR11 in the cark1 mutant is able to functionally complement the ABA sensitivity. CARK1 positively regulates ABA-responsive gene expression and enhances RCAR3/RCAR11’s inhibition to Clade A PP2C. Taken together, our studies strongly support the functional significance of CARK1 in positively regulating ABA signaling via phosphorylation on RCAR3/RCAR11 in Arabidopsis.
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spelling pubmed-60062482018-06-20 CARK1 mediates ABA signaling by phosphorylation of ABA receptors Zhang, Liang Li, Xiaoyi Li, Dekuan Sun, Yuna Li, Ying Luo, Qin Liu, Zhibin Wang, Jianmei Li, Xufeng Zhang, Hong Lou, Zhiyong Yang, Yi Cell Discov Article The function of abscisic acid (ABA) is mediated by its receptors termed RCARs/PYR1/PYLs. Modulation of ABA signaling is vital for plant growth and development. The RCAR-PP2C-SnRK2 regulatory modules have been defined as the core components in ABA signaling. However, it is still not clear whether and how the ABA receptors could be modified at the initial post-translational stage to fine-tune ABA transduction pathway. Here we identify and characterize the putative receptor-like cytoplasmic kinase (RLCK) in Arabidopsis named CARK1, which interacts with RCAR3 (PYL8) and RCAR11 (PYR1) in the manner of phosphorylation. Structural studies of CARK1 revealed the critical active site, N204, which accounts for the kinase activity and the direct interaction with RCAR3/RCAR11. CARK1 phosphorylates RCAR3/RCAR11 at one conserved threonine site, T77/T78. Our genetic analyses further demonstrated that CARK1 positively regulates ABA-mediated physiological responses and overexpression of CARK1 in Arabidopsis distinctly promotes the drought resistance. Moreover, the phosphor-mimic form of RCAR11 in the cark1 mutant is able to functionally complement the ABA sensitivity. CARK1 positively regulates ABA-responsive gene expression and enhances RCAR3/RCAR11’s inhibition to Clade A PP2C. Taken together, our studies strongly support the functional significance of CARK1 in positively regulating ABA signaling via phosphorylation on RCAR3/RCAR11 in Arabidopsis. Nature Publishing Group UK 2018-06-19 /pmc/articles/PMC6006248/ /pubmed/29928509 http://dx.doi.org/10.1038/s41421-018-0029-y Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Zhang, Liang
Li, Xiaoyi
Li, Dekuan
Sun, Yuna
Li, Ying
Luo, Qin
Liu, Zhibin
Wang, Jianmei
Li, Xufeng
Zhang, Hong
Lou, Zhiyong
Yang, Yi
CARK1 mediates ABA signaling by phosphorylation of ABA receptors
title CARK1 mediates ABA signaling by phosphorylation of ABA receptors
title_full CARK1 mediates ABA signaling by phosphorylation of ABA receptors
title_fullStr CARK1 mediates ABA signaling by phosphorylation of ABA receptors
title_full_unstemmed CARK1 mediates ABA signaling by phosphorylation of ABA receptors
title_short CARK1 mediates ABA signaling by phosphorylation of ABA receptors
title_sort cark1 mediates aba signaling by phosphorylation of aba receptors
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6006248/
https://www.ncbi.nlm.nih.gov/pubmed/29928509
http://dx.doi.org/10.1038/s41421-018-0029-y
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