Dataset Information

Reciprocal regulation of the TOR kinase and ABA receptor balances plant growth and stress response

ABSTRACT: We found that TOR kinase regulates the plant environmental stress responses through phosphorylation at a conserved serine residue of Abscisic acid receptor PYR1/PYLs/RCARs. The phosphorylation inhibits the function of PYLs and prevents the binding of PYLs to abscisic acid and its downstream substrates of PP2C, which blocks the ABA and stress signaling. Our results suggest that plant utilizes this mechanism as a hub to regulate the ABA-mediate stress responses and growth recovery

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Whole Plant

SUBMITTER: Chuan-Chih Hsu

LAB HEAD: Jian-Kang Zhu

PROVIDER: PXD003746 | Pride | 2017-12-01

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

Items per page:

1 - 5 of 126

Publications

Reciprocal Regulation of the TOR Kinase and ABA Receptor Balances Plant Growth and Stress Response.

Wang Pengcheng P Zhao Yang Y Li Zhongpeng Z Hsu Chuan-Chih CC Liu Xue X Fu Liwen L Hou Yueh-Ju YJ Du Yanyan Y Xie Shaojun S Zhang Chunguang C Gao Jinghui J Cao Minjie M Huang Xiaosan X Zhu Yingfang Y Tang Kai K Wang Xingang X Tao W Andy WA Xiong Yan Y Zhu Jian-Kang JK

Molecular cell 20171228 1

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 di ...[more]

PMID: 29290610

Similar Datasets

Project description:This model is from the article: A thermodynamic switch modulates abscisic acid receptor sensitivity. Dupeux F, Santiago J, Betz K, Twycross J, Park SY, Rodriguez L, Gonzalez-Guzman M, Jensen MR, Krasnogor N, Blackledge M, Holdsworth M, Cutler SR, Rodriguez PL, Márquez JA EMBO J. [2011 Oct; Volume: 30 (Issue: 20 )] Page info: 4171-84 21847091 , Abstract: Abscisic acid (ABA) is a key hormone regulating plant growth, development and the response to biotic and abiotic stress. ABA binding to pyrabactin resistance (PYR)/PYR1-like (PYL)/Regulatory Component of Abscisic acid Receptor (RCAR) intracellular receptors promotes the formation of stable complexes with certain protein phosphatases type 2C (PP2Cs), leading to the activation of ABA signalling. The PYR/PYL/RCAR family contains 14 genes in Arabidopsis and is currently the largest plant hormone receptor family known; however, it is unclear what functional differentiation exists among receptors. Here, we identify two distinct classes of receptors, dimeric and monomeric, with different intrinsic affinities for ABA and whose differential properties are determined by the oligomeric state of their apo forms. Moreover, we find a residue in PYR1, H60, that is variable between family members and plays a key role in determining oligomeric state. In silico modelling of the ABA activation pathway reveals that monomeric receptors have a competitive advantage for binding to ABA and PP2Cs. This work illustrates how receptor oligomerization can modulate hormonal responses and more generally, the sensitivity of a ligand-dependent signalling system. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not. To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

			Action	DRS
	013116-020216-021616-WT-ABA-MaxQuant.zip	Other
	013116-WT-10.msf	Msf
	013116-WT-10.pdResult	Other
	013116-WT-10.raw	Raw
	013116-WT-13.msf	Msf