Monomerization of abscisic acid receptors through CARKs-mediated phosphorylation

Bibliographische Detailangaben
Veröffentlicht in:	The New phytologist. - 1979. - 235(2022), 2 vom: 20. Juli, Seite 533-549
1. Verfasser:	Li, Xiaoyi (VerfasserIn)
Weitere Verfasser:	Xie, Yiting, Zhang, Qian, Hua, Xinyue, Peng, Lu, Li, Kexuan, Yu, Qin, Chen, Yihong, Yao, Huan, He, Juan, Huang, Yaling, Wang, Ruolin, Wang, Tao, Wang, Jianmei, Li, Xufeng, Yang, Yi
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2022
Zugriff auf das übergeordnete Werk:	The New phytologist
Schlagworte:	Journal Article Research Support, Non-U.S. Gov't ABA receptor ABI5 CARKs abscisic acid (ABA) de-dimerization phosphorylation Arabidopsis Proteins Abscisic Acid 72S9A8J5GW

Beschreibung
Zusammenfassung:	© 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation. Cytosolic ABA Receptor Kinases (CARKs) play a pivotal role in abscisic acid (ABA)-dependent pathway in response to dehydration, but their regulatory mechanism in ABA signaling remains unexplored. In this study, we showed that CARK4/5 of CARK family physically interacted with ABA receptors (RCARs/PYR1/PYLs), including RCAR3, RCAR11-RCAR14, while CARK2/7/11 only interacted with RCAR11-RCAR14, but not RCAR3. It indicates that the members in CARK family function redundantly and differentially in ABA signaling. RCAR12 can form heterodimer with RCAR3 in vitro and in vivo. Moreover, the members of CARK family can form homodimer or heterodimer in a kinase activity dependent manner. ITC (isothermal titration calorimetry) analysis demonstrated that the phosphorylation of RCAR12 by CARK1 enhanced the ABA binding affinity. The phosphor-mimic RCAR12T105D significantly displayed ABA-induced inhibition of the phosphatase ABI1 (ABA insensitive 1) activity, leading to upregulation of ABA-responsive genes RD29A and RD29B in cark157:RCAR12T105D transgenic plants, which exhibited ABA hypersensitive phenotype. The transcription factor ABI5 (ABA insensitive 5) activates the transcriptions of CARK1 and CARK3 by binding to ABA-response elements (ABREs) of their promoters. Collectively, our data imply that the dimeric CARKs phosphorylate homodimer or heterodimer ABA receptors, leading to monomerization for triggering ABA responses in Arabidopsis
Beschreibung:	Date Completed 17.06.2022 Date Revised 27.06.2022 published: Print-Electronic Citation Status MEDLINE
ISSN:	1469-8137
DOI:	10.1111/nph.18149