| Literature DB >> 29290610 |
Pengcheng Wang1, Yang Zhao2, Zhongpeng Li2, Chuan-Chih Hsu3, Xue Liu2, Liwen Fu2, Yueh-Ju Hou4, Yanyan Du2, Shaojun Xie4, Chunguang Zhang4, Jinghui Gao4, Minjie Cao2, Xiaosan Huang4, Yingfang Zhu1, Kai Tang1, Xingang Wang4, W Andy Tao3, Yan Xiong5, Jian-Kang Zhu6.
Abstract
As sessile organisms, plants must adapt to variations in the environment. Environmental stress triggers various responses, including growth inhibition, mediated by the plant hormone abscisic acid (ABA). The mechanisms that integrate stress responses with growth are poorly understood. Here, we discovered that the Target of Rapamycin (TOR) kinase phosphorylates PYL ABA receptors at a conserved serine residue to prevent activation of the stress response in unstressed plants. This phosphorylation disrupts PYL association with ABA and with PP2C phosphatase effectors, leading to inactivation of SnRK2 kinases. Under stress, ABA-activated SnRK2s phosphorylate Raptor, a component of the TOR complex, triggering TOR complex dissociation and inhibition. Thus, TOR signaling represses ABA signaling and stress responses in unstressed conditions, whereas ABA signaling represses TOR signaling and growth during times of stress. Plants utilize this conserved phospho-regulatory feedback mechanism to optimize the balance of growth and stress responses.Entities:
Keywords: ABA receptor; Raptor; SnRK2; Target of Rapamycin; abscisic acid; phosphorylation
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Year: 2017 PMID: 29290610 PMCID: PMC5772982 DOI: 10.1016/j.molcel.2017.12.002
Source DB: PubMed Journal: Mol Cell ISSN: 1097-2765 Impact factor: 17.970