Evidence map›Paper›PMID 36943771›Full record

ArticleThe Plant cell2023

14-3-3 proteins facilitate the activation of MAP kinase cascades by upstream immunity-related kinases.

Xiaojing Dong, Feng Feng, Yangjun Li, Lin Li, She Chen, Jian-Min Zhou

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  14. G-Box Factors 14-3-3 Proteins Negatively RegulatePlants (Basel, Switzerland) · 2025
    Article
  15. Journal of agricultural and food chemistry · 2025
    Article
  16. Review
  17. An Insect Effector Mimics Its Host Immune Regulator to Undermine Plant Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  18. Article
  19. Article
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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 3 institutions in 2 countries.

Xiaojing DongState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0002-9807-0044
Feng FengDepartment of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.ORCID 0000-0003-1382-305X
Yangjun LiState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0002-1547-4159
Lin LiNational Institute of Biological Sciences, Beijing 102206, China.ORCID 0000-0001-6353-8594
She ChenNational Institute of Biological Sciences, Beijing 102206, China.ORCID 0000-0002-0830-3263
Jian-Min ZhouState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0002-9943-2975
Chinese Academy of Sciences · CNNational Institute of Biological Sciences, Beijing · CNOklahoma State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of mitogen-activated protein kinase (MAP kinase) cascades is essential for plant immunity. Upon activation by surface-localized immune receptors, receptor-like cytoplasmic kinases (RLCKs) in the cytoplasm phosphorylate MAP kinase kinase kinases (MAPKKKs) to initiate MAP kinase activation. Surprisingly, we found that both the phosphorylation of Arabidopsis (Arabidopsis thaliana) MAPKKKs and the subsequent activation of MAP kinase cascades require the λ and κ isoforms of 14-3-3 proteins, which directly interact with multiple RLCKs and MAPKKKs. The N- and C-termini of MAPKKK5 interact intramolecularly to inhibit the access to the C terminus by RLCKs, whereas the 14-3-3 proteins relieve this inhibition and facilitate the interaction of RLCKs with the C-terminus of MAPKKK5. This enables the phosphorylation of MAPKK5 at Ser599 and Ser682, thus promoting MAP kinase activation and enhancing plant disease resistance. Our study reveals a role of 14-3-3 proteins as scaffolds and activators in the regulation of the RLCK-MAPKKK5 module and provides insight into the mechanism of plant immune signaling.

Indexed as

ArabidopsisMitogen-Activated Protein Kinases14-3-3 ProteinsMAP Kinase Kinase Kinase 5MAP Kinase Signaling SystemPhosphorylationPlants14-3-3 ProteinsMAP Kinase Kinase Kinase 5Mitogen-Activated Protein Kinases

Identifiers

PMID36943771
PMCPMC10226567
OpenAlexW4328048610

What OpenQuestion holds

Textmetadata
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.