Evidence map›Paper›PMID 41723113›Full record

ArticleNature communications2026

A phosphorylation-dependent ubiquitination switch orchestrates nuclear immune reprogramming upon chitin perception.

Chongyang Zhang, Pavinee Suttiviriya, Ruyi Wang, Feng He, Hui Tao, Debao Wang, Jisong Wang, Liang Fang, Zeyun Hao, Xiaoman You and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
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

13 authors.

Chongyang ZhangState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.ORCID http://orcid.org/0009-0002-2284-1102
Pavinee SuttiviriyaDepartment of Plant Pathology, The Ohio State University, Columbus, OH, USA.
Ruyi WangState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-9940-5918
Feng HeState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Hui TaoState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Debao WangState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-2567-6635
Jisong WangState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Liang FangState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Zeyun HaoState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Xiaoman YouState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Wei LiDepartment of Plant Pathology, The Ohio State University, Columbus, OH, USA.
Guo-Liang WangDepartment of Plant Pathology, The Ohio State University, Columbus, OH, USA.ORCID http://orcid.org/0000-0001-8877-3064
Yuese NingState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China. ningyuese@caas.cn.ORCID http://orcid.org/0000-0003-1675-3114

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32161143009National Natural Science Foundation of China (National Science Foundation of China) 32402396National Natural Science Foundation of China (National Science Foundation of China) U24A20388
6 · The paper itself

Abstract

The 14-3-3 proteins, a highly conserved class in all eukaryotes, are widely associated with plant growth and stress responses. However, their role in plant immunity and its regulatory mechanisms remains elusive. Here, we show that two homologous rice 14-3-3 proteins, OsGF14f and OsGF14c, function redundantly to enhance rice resistance against Magnaporthe oryzae. The E3 ligase OsPUB20 targets OsGF14f and OsGF14c for ubiquitination and 26S proteasome-mediated degradation, thereby negatively regulating rice immunity. Remarkably, chitin perception activates the receptor-like cytoplasmic kinase OsRLCK185 that phosphorylates OsPUB20 at Thr153, which stabilizes OsGF14f and enhances rice blast resistance. Furthermore, during M. oryzae infection, OsGF14f translocates into the nucleus, where it facilitates the degradation of OsWRKY42, a transcription factor that negatively regulates defense responses. Collectively, our findings reveal a phosphorylation-dependent ubiquitination switch that links cell surface chitin perception to nuclear immune reprogramming during M. oryzae invasion.

Indexed as

14-3-3 ProteinsChitinOryzaPlant ImmunityPlant ProteinsAscomycotaCell NucleusDisease ResistanceMagnaporthePhosphorylationPlant DiseasesProteasome Endopeptidase ComplexUbiquitinationUbiquitin-Protein Ligases14-3-3 ProteinsChitinPlant ProteinsProteasome Endopeptidase ComplexUbiquitin-Protein Ligases

Identifiers

PMID41723113
PMCPMC13036091

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.