Author
Listed:
- 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
National Center for Plant Gene Research)
- 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
National Center for Plant Gene Research)
- Zhizhong Gong
(State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University
National Center for Plant Gene Research)
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.
Suggested Citation
Lingyao Kong & Jinkui Cheng & Yujuan Zhu & Yanglin Ding & Jingjing Meng & Zhizhong Chen & Qi Xie & Yan Guo & Jigang Li & Shuhua Yang & Zhizhong Gong, 2015.
"Degradation of the ABA co-receptor ABI1 by PUB12/13 U-box E3 ligases,"
Nature Communications, Nature, vol. 6(1), pages 1-13, December.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9630
DOI: 10.1038/ncomms9630
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Cited by:
- Chuanzhong Zhang & Hongru Wang & Xiaojie Tian & Xinyan Lin & Yunfei Han & Zhongmin Han & Hanjing Sha & Jia Liu & Jianfeng Liu & Jian Zhang & Qingyun Bu & Jun Fang, 2024.
"A transposon insertion in the promoter of OsUBC12 enhances cold tolerance during japonica rice germination,"
Nature Communications, Nature, vol. 15(1), pages 1-16, December.
- Jiaojiao Bai & Yuanyuan Zhou & Jianhang Sun & Kexin Chen & Yufang Han & Ranran Wang & Yanmin Zou & Mingshuo Du & Dongping Lu, 2023.
"BIK1 protein homeostasis is maintained by the interplay of different ubiquitin ligases in immune signaling,"
Nature Communications, Nature, vol. 14(1), pages 1-14, December.
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