Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor
The Arabidopsis immune receptor FLS2 perceives bacterial flagellin epitope flg22 to activate defenses through the central cytoplasmic kinase BIK1. The heterotrimeric G proteins composed of the non-canonical Gα protein XLG2, the Gβ protein AGB1, and the Gγ proteins AGG1 and AGG2 are required for FLS2...
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eLife Sciences Publications Ltd
2016-04-01
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Online Access: | https://elifesciences.org/articles/13568 |
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author | Xiangxiu Liang Pingtao Ding Kehui Lian Jinlong Wang Miaomiao Ma Lin Li Lei Li Meng Li Xiaojuan Zhang She Chen Yuelin Zhang Jian-Min Zhou |
author_facet | Xiangxiu Liang Pingtao Ding Kehui Lian Jinlong Wang Miaomiao Ma Lin Li Lei Li Meng Li Xiaojuan Zhang She Chen Yuelin Zhang Jian-Min Zhou |
author_sort | Xiangxiu Liang |
collection | DOAJ |
description | The Arabidopsis immune receptor FLS2 perceives bacterial flagellin epitope flg22 to activate defenses through the central cytoplasmic kinase BIK1. The heterotrimeric G proteins composed of the non-canonical Gα protein XLG2, the Gβ protein AGB1, and the Gγ proteins AGG1 and AGG2 are required for FLS2-mediated immune responses through an unknown mechanism. Here we show that in the pre-activation state, XLG2 directly interacts with FLS2 and BIK1, and it functions together with AGB1 and AGG1/2 to attenuate proteasome-mediated degradation of BIK1, allowing optimum immune activation. Following the activation by flg22, XLG2 dissociates from AGB1 and is phosphorylated by BIK1 in the N terminus. The phosphorylated XLG2 enhances the production of reactive oxygen species (ROS) likely by modulating the NADPH oxidase RbohD. The study demonstrates that the G proteins are directly coupled to the FLS2 receptor complex and regulate immune signaling through both pre-activation and post-activation mechanisms. |
first_indexed | 2024-04-12T02:14:31Z |
format | Article |
id | doaj.art-5a9842c5b05b4fd8963629617331a4b4 |
institution | Directory Open Access Journal |
issn | 2050-084X |
language | English |
last_indexed | 2024-04-12T02:14:31Z |
publishDate | 2016-04-01 |
publisher | eLife Sciences Publications Ltd |
record_format | Article |
series | eLife |
spelling | doaj.art-5a9842c5b05b4fd8963629617331a4b42022-12-22T03:52:17ZengeLife Sciences Publications LtdeLife2050-084X2016-04-01510.7554/eLife.13568Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptorXiangxiu Liang0Pingtao Ding1https://orcid.org/0000-0002-3535-6053Kehui Lian2Jinlong Wang3Miaomiao Ma4Lin Li5Lei Li6Meng Li7Xiaojuan Zhang8She Chen9Yuelin Zhang10Jian-Min Zhou11https://orcid.org/0000-0002-9943-2975State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, ChinaDepartment of Botany, University of British Columbia, Vancouver, CanadaDepartment of Botany, University of British Columbia, Vancouver, CanadaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, ChinaNational Institute of Biological Sciences, Beijing, ChinaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, ChinaNational Institute of Biological Sciences, Beijing, ChinaDepartment of Botany, University of British Columbia, Vancouver, CanadaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, ChinaThe Arabidopsis immune receptor FLS2 perceives bacterial flagellin epitope flg22 to activate defenses through the central cytoplasmic kinase BIK1. The heterotrimeric G proteins composed of the non-canonical Gα protein XLG2, the Gβ protein AGB1, and the Gγ proteins AGG1 and AGG2 are required for FLS2-mediated immune responses through an unknown mechanism. Here we show that in the pre-activation state, XLG2 directly interacts with FLS2 and BIK1, and it functions together with AGB1 and AGG1/2 to attenuate proteasome-mediated degradation of BIK1, allowing optimum immune activation. Following the activation by flg22, XLG2 dissociates from AGB1 and is phosphorylated by BIK1 in the N terminus. The phosphorylated XLG2 enhances the production of reactive oxygen species (ROS) likely by modulating the NADPH oxidase RbohD. The study demonstrates that the G proteins are directly coupled to the FLS2 receptor complex and regulate immune signaling through both pre-activation and post-activation mechanisms.https://elifesciences.org/articles/13568plant immunityoxidative burstphosphorylationheterotrimeric G proteins |
spellingShingle | Xiangxiu Liang Pingtao Ding Kehui Lian Jinlong Wang Miaomiao Ma Lin Li Lei Li Meng Li Xiaojuan Zhang She Chen Yuelin Zhang Jian-Min Zhou Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor eLife plant immunity oxidative burst phosphorylation heterotrimeric G proteins |
title | Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor |
title_full | Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor |
title_fullStr | Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor |
title_full_unstemmed | Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor |
title_short | Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor |
title_sort | arabidopsis heterotrimeric g proteins regulate immunity by directly coupling to the fls2 receptor |
topic | plant immunity oxidative burst phosphorylation heterotrimeric G proteins |
url | https://elifesciences.org/articles/13568 |
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