Evidence map›Paper›PMID 27043937›Full record

ArticleeLife2016

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 and 2 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
70.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

124 citing papers in PubMed, 277 citations in OpenAlex.

  1. Mechanisms and balanced regulation of plant immunity.Nature reviews. Molecular cell biology · 2026
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  17. Overexpression ofPlants (Basel, Switzerland) · 2024
    Article
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  20. Article

64 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 2 countries.

Xiangxiu LiangState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Pingtao DingDepartment of Botany, University of British Columbia, Vancouver, Canada.ORCID http://orcid.org/0000-0002-3535-6053
Kehui LianDepartment of Botany, University of British Columbia, Vancouver, Canada.
Jinlong WangState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Miaomiao MaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Lin LiNational Institute of Biological Sciences, Beijing, China.
Lei LiState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Meng LiState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Xiaojuan ZhangState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
She ChenNational Institute of Biological Sciences, Beijing, China.
Yuelin ZhangDepartment of Botany, University of British Columbia, Vancouver, Canada.
Jian-Min ZhouState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-9943-2975
Chinese Academy of Sciences · CNUniversity of British Columbia · CANational Institute of Biological Sciences, Beijing · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Antigens, BacterialArabidopsisArabidopsis ProteinsFlagellinHeterotrimeric GTP-Binding ProteinsProtein BindingProtein KinasesReactive Oxygen SpeciesSignal TransductionAntigens, BacterialArabidopsis ProteinsFlagellinFLS2 protein, ArabidopsisHeterotrimeric GTP-Binding ProteinsProtein KinasesReactive Oxygen Speciescell biologyheterotrimeric G proteins<i>a. thaliana</i>oxidative burstphosphorylationplant biologyplant immunity

Identifiers

PMID27043937
PMCPMC4846371
OpenAlexW2339535719

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.