Evidence map›Paper›PMID 40991707›Full record

ArticleScience advances2025

The MC4-La1 cleavage module restricts plant virus infection by integrating R-motif-mediated defense mRNA translation.

Qinglin Pi, Rujian Hu, Ning Yue, Zhihao Jiang, Jing Wei, Yanlin Chen, Meng Yang, Wen Song, Yongliang Zhang, Jinlong Wang and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

11 authors.

Qinglin PiState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.ORCID 0000-0002-1446-1209
Rujian HuState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.ORCID 0000-0002-9744-2272
Ning YueState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.ORCID 0000-0003-2003-9466
Zhihao JiangState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.ORCID 0000-0002-2688-6255
Jing WeiState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
Yanlin ChenState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
Meng YangState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.ORCID 0000-0002-1032-6800
Wen SongState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
Yongliang ZhangState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.ORCID 0000-0002-6790-1044
Jinlong WangState Key Laboratory of Plant Genomics, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0001-9739-4525
Dawei LiState Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.ORCID 0000-0003-4133-1263

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plant cysteine protease metacaspases are structural homologs of animal caspases and play pivotal roles under biotic and abiotic stresses. However, whether metacaspases and purine-rich element (R-motif)-mediated defense messenger RNA translation are involved in plant antiviral immunity remains elusive. Here, we report that barley stripe mosaic virus (BSMV) infection activates metacaspase 4 (MC4) to cleave the RNA binding protein lupus autoantigen 1 (La1) behind residue arginine-448. The cleaved La1

Indexed as

Cysteine EndopeptidasesNicotianaPlant VirusesRNA-Binding ProteinsViral Nonstructural ProteinsDisease ResistanceEnzyme ActivationGene Expression Regulation, PlantHost-Pathogen InteractionsCysteine Endopeptidasesgamma(b) protein, Barley stripe mosaic virusRNA-Binding ProteinsViral Nonstructural Proteins

Identifiers

PMID40991707
PMCPMC12459463

What OpenQuestion holds

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LicenceCC BY-NC
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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.