Evidence map›Paper›PMID 29545645›Full record

ArticleCell research2018

Ligand-triggered de-repression of Arabidopsis heterotrimeric G proteins coupled to immune receptor kinases.

Xiangxiu Liang, Miaomiao Ma, Zhaoyang Zhou, Jinlong Wang, Xinru Yang, Shaofei Rao, Guozhi Bi, Lin Li, Xiaojuan Zhang, Jijie Chai and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Cell research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
18.9field-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

47 citing papers in PubMed, 120 citations in OpenAlex.

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  13. TheInternational journal of molecular sciences · 2023
    Article
  14. An atypical heterotrimeric Gα and its interactome suggest an extra-large role in overcoming abiotic and biotic stress.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 1 country.

Xiangxiu LiangState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China.
Miaomiao MaState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China.
Zhaoyang ZhouState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China.
Jinlong WangState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China.
Xinru YangCenter for Plant Biology, School of Life Sciences, Tsinghua University, 100084, Beijing, China.
Shaofei RaoState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China.
Guozhi BiState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China.
Lin LiNational Institute of Biological Sciences, 102206, Beijing, China.
Xiaojuan ZhangState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China.
Jijie ChaiCenter for Plant Biology, School of Life Sciences, Tsinghua University, 100084, Beijing, China.
She ChenNational Institute of Biological Sciences, 102206, Beijing, China.
Jian-Min ZhouState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101, Beijing, China. jmzhou@genetics.ac.cn.ORCID 0000-0002-9943-2975
Chinese Academy of Sciences · CNNational Institute of Biological Sciences, Beijing · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis heterotrimeric G proteins regulate diverse processes by coupling to single-transmembrane receptors. One such receptor is the FLS2 receptor kinase, which perceives bacterial flagellin epitope flg22 to activate immunity through a class of cytoplasmic kinases called BIK1/PBLs. Unlike animal and fungal heterotrimeric G proteins that are activated by a ligand-induced guanine nucleotide exchange activity of seven-transmembrane G protein-coupled receptors (GPCRs), plant heterotrimeric G proteins are self-activating. How plant receptors regulate heterotrimeric G proteins in response to external ligands remains unknown. Here we show that RGS1, a GTPase accelerating protein, maintains Arabidopsis G proteins in an inactive state in complex with FLS2. Activation of FLS2 by flg22 induces a BIK1/PBL-mediated phosphorylation of RGS1 at Ser428 and Ser431 and that promotes RGS1 dissociation from the FLS2-G protein complex. This relieves G proteins from the RGS1-mediated repression and enables positive regulation of immune signaling. We additionally show that RGS1 is similarly regulated by multiple immune receptors. Our results uncover ligand-induced de-repression as a mechanism for G protein signaling in plants that is distinct from previously reported mechanism underlying the activation of heterotrimeric G proteins in other systems.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsFlagellinHeterotrimeric GTP-Binding ProteinsLigandsPhosphorylationPhosphoserinePlant ImmunityProtein BindingProtein KinasesReceptors, Pattern RecognitionSignal TransductionArabidopsis ProteinsFlagellinHeterotrimeric GTP-Binding ProteinsLigandsPhosphoserineProtein KinasesReceptors, Pattern Recognition

Identifiers

PMID29545645
PMCPMC5951851
OpenAlexW2794098854

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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.