Evidence map›Paper›PMID 39952938›Full record

ArticleNature communications2025

Proteasomes accumulate in the plant apoplast where they participate in microbe-associated molecular pattern (MAMP)-triggered pathogen defense.

Hana Zand Karimi, Kuo-En Chen, Marilee Karinshak, Xilin Gu, Jason K Sello, Richard D Vierstra

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Beyond Resistance Genes: Silencing Susceptibility.International journal of molecular sciences · 2026
    Review
  2. Review
  3. Proteomic snapshot of pattern triggered immunity in the Arabidopsis leaf apoplast.The Plant journal : for cell and molecular biology · 2025
    Article
  4. Review
  5. Streamline Protocol forPlant direct · 2025
    Article
  6. 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.

Hana Zand KarimiDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0003-4012-713X
Kuo-En ChenDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0003-0517-9401
Marilee KarinshakDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Xilin GuDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.ORCID http://orcid.org/0000-0002-5441-7958
Jason K SelloDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.ORCID http://orcid.org/0000-0001-6263-7902
Richard D VierstraDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA. rdvierstra@wustl.edu.ORCID http://orcid.org/0000-0003-0210-3516

Funding

Autophagic Clearance of Proteasomes and CDC48 as Models for Amyloidogenic Protein Quality Control.R01GM124452 · NIGMS · WASHINGTON UNIVERSITY · PI JEZ, JOSEPH MARTIN · 2018 to 2025
$2.4M
NIGMS NIH HHS R01 GM124452U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM-124452
6 · The paper itself

Abstract

Akin to mammalian extracellular fluids, the plant apoplastic fluid (APF) contains a unique collection of proteins, RNAs, and vesicles that drive many physiological processes ranging from cell wall assembly to defense against environmental challenges. Using an improved method to enrich for the Arabidopsis APF, we better define its composition and discover that the APF harbors active proteasomes though microscopic detection, proteasome-specific activity and immunological assays, and mass spectrometry showing selective enrichment of the core protease. Functional analysis of extracellular (ex)-proteasomes reveals that they help promote basal pathogen defense through proteolytic release of microbe-associated molecular patterns (MAMPs) such as flg22 from bacterial flagellin that induce protective reactive-oxygen-species (ROS) bursts. Flagellin-triggered ROS is also strongly suppressed by the enigmatic Pseudomonas syringae virulence effector syringolin-A that blocks ex-proteasome activity. Collectively, we provide a deep catalog of apoplast proteins and evidence that ex-proteasomes participate in the evolving arms race between pathogens and their plant hosts.

Indexed as

ArabidopsisArabidopsis ProteinsPathogen-Associated Molecular Pattern MoleculesProteasome Endopeptidase ComplexBacterial ProteinsFlagellinHost-Pathogen InteractionsPeptides, CyclicPlant DiseasesPlant ImmunityPseudomonas syringaeReactive Oxygen SpeciesArabidopsis ProteinsBacterial ProteinsFlagellinPathogen-Associated Molecular Pattern MoleculesPeptides, CyclicProteasome Endopeptidase ComplexReactive Oxygen Speciessyringolin A

Identifiers

PMID39952938
PMCPMC11829042

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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.