ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation
| 作者： |
Feifei Yu, Lijuan Lou, Miaomiao Tian, Qingliang Li, Yanglin Ding, Xiaoqiang Cao, Yaorong Wu, Borja Belda-Palazon, Pedro L. Rodriguez, Shuhua Yang, Qi Xie |
| 刊物名称： |
Molecular Plant |
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| 发表年度： |
2016-11-21 |
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| 摘要： |
The recent discovery of PYR/PYL/RCAR-type ABA receptors has been one of most significant advances in plant science. In mammals, endosome sorting acts as an important pathway to down-regulate different types of receptors, but this kind of regulation of hormone signaling is poorly understood in plants. Here, we report that an ubiquitin E2-like protein, VPS23A, also a key component of ESCRT-I, negatively regulates ABA signaling. VPS23A has epistatic relation with PYR/PYL/RCAR type ABA receptors and deletion of VPS23A enhances the activity of key kinase OST1 in ABA signaling pathway under ABA treatment. Moreover, VPS23A interacts with PYR1/PYLs and K63-linked diubiquitin, and PYL4 possesses K63-linked ubiquitinated modification in vivo. VPS23A affects the subcellular localization of PYR1 and stability of the PYL4 by vps23a mutant analysis. These findings supports that VPS23A affects PYR1/PYL4 via vacuole-mediated degradation besides 26S proteasome system, further strengthen our understanding of both the turnover of ABA receptors and ESCRTs in plant hormone signaling. |
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