Evidence map›Paper›PMID 33980819›Full record

ArticleNature communications2021

S-acylation of P2K1 mediates extracellular ATP-induced immune signaling in Arabidopsis.

Dongqin Chen, Fengsheng Hao, Huiqi Mu, Nagib Ahsan, Jay J Thelen, Gary Stacey

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
11.5field-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

43 citing papers in PubMed, 68 citations in OpenAlex.

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  9. Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025
    Article
  10. Review
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  20. DecodingPlants (Basel, Switzerland) · 2024
    Article
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

6 authors at 2 institutions in 2 countries.

Dongqin ChenState Key Laboratory of Agrobiotechnology, College of Plant Protection, China Agricultural University, Beijing, China. chendq@cau.edu.cn.ORCID 0000-0002-4715-4491
Fengsheng HaoState Key Laboratory of Agrobiotechnology, College of Plant Protection, China Agricultural University, Beijing, China.
Huiqi MuState Key Laboratory of Agrobiotechnology, College of Plant Protection, China Agricultural University, Beijing, China.
Nagib AhsanDivision of Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, MO, USA.
Jay J ThelenDivision of Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, MO, USA.ORCID 0000-0001-5995-1562
Gary StaceyDivision of Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, MO, USA. staceyg@missouri.edu.ORCID 0000-0001-5914-2247
China Agricultural University · CNUniversity of Missouri · US

Funding

DORN1 defines a new family of receptor kinase purinoreceptors (P2K)R01GM121445 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI STACEY, GARY · 2017 to 2024
$2.5M
NIGMS NIH HHS R01 GM121445
6 · The paper itself

Abstract

S-acylation is a reversible protein post-translational modification mediated by protein S-acyltransferases (PATs). How S-acylation regulates plant innate immunity is our main concern. Here, we show that the plant immune receptor P2K1 (DORN1, LecRK-I.9; extracellular ATP receptor) directly interacts with and phosphorylates Arabidopsis PAT5 and PAT9 to stimulate their S-acyltransferase activity. This leads, in a time-dependent manner, to greater S-acylation of P2K1, which dampens the immune response. pat5 and pat9 mutants have an elevated extracellular ATP-induced immune response, limited bacterial invasion, increased phosphorylation and decreased degradation of P2K1 during immune signaling. Mutation of S-acylated cysteine residues in P2K1 results in a similar phenotype. Our study reveals that S-acylation effects the temporal dynamics of P2K1 receptor activity, through autophosphorylation and protein degradation, suggesting an important role for this modification in regulating the ability of plants in respond to external stimuli.

Indexed as

Plant ImmunityAcylationAcyltransferasesAdenosine TriphosphateArabidopsisArabidopsis ProteinsMutationPhosphorylationPlants, Genetically ModifiedProtein BindingProtein KinasesReceptors, Pattern RecognitionReceptors, Purinergic P2Signal TransductionTime FactorsAcyltransferasesAdenosine TriphosphateArabidopsis ProteinsLecRK-I.9 protein, ArabidopsisProtein KinasesReceptors, Pattern RecognitionReceptors, Purinergic P2

Identifiers

PMID33980819
PMCPMC8115640
OpenAlexW3160896491

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.