Degradation of the ABA co-receptor ABI1 by PUB12/13 U-box E3 ligases

Lingyao Kong, Jinkui Cheng, Yujuan Zhu, Yanglin Ding, Jingjing Meng, Zhizhong Chen, Qi Xie, Yan Guo, Jigang Li, Shuhua Yang and Zhizhong Gong ()
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Lingyao Kong: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Jinkui Cheng: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Yujuan Zhu: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Yanglin Ding: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Jingjing Meng: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Zhizhong Chen: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Qi Xie: State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences
Yan Guo: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Jigang Li: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Shuhua Yang: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
Zhizhong Gong: State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University

Nature Communications, 2015, vol. 6, issue 1, 1-13

Abstract: Abstract Clade A protein phosphatase 2Cs (PP2Cs) are abscisic acid (ABA) co-receptors that block ABA signalling by inhibiting the downstream protein kinases. ABA signalling is activated after PP2Cs are inhibited by ABA-bound PYR/PYL/RCAR ABA receptors (PYLs) in Arabidopsis. However, whether these PP2Cs are regulated by other factors remains unknown. Here, we report that ABI1 (ABA-INSENSITIVE 1) can interact with the U-box E3 ligases PUB12 and PUB13, but is ubiquitinated only when it interacts with ABA receptors in an in vitro assay. A mutant form of ABI1-1 that is unable to interact with PYLs is more stable than the wild-type protein. Both ABI1 degradation and all tested ABA responses are reduced in pub12 pub13 mutants compared with the wild type. Introducing the abi1-3 loss-of-function mutation into pub12 pub13 mutant recovers the ABA-insensitive phenotypes of the pub12 pub13 mutant. We thus uncover an important regulatory mechanism for regulating ABI1 levels by PUB12 and PUB13.

Date: 2015
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DOI: 10.1038/ncomms9630

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