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Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor
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
eLIFE
Abstract
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.
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论文编号: |
DOI:10.7554/eLife.13568 |
论文题目: |
Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor |
英文论文题目: |
Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor |
第一作者: |
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 |
英文第一作者: |
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 |
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2016-04-08 |
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摘要: |
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. |
英文摘要: |
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. |
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eLIFE |
英文刊物名称: |
eLIFE |
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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. DOI:10.7554/eLife.13568 |
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