IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-56594-3.html
   My bibliography  Save this article

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

Author

Listed:
  • Hana Zand Karimi

    (Washington University in St. Louis
    Pfizer Pharmaceuticals)

  • Kuo-En Chen

    (Washington University in St. Louis)

  • Marilee Karinshak

    (Washington University in St. Louis)

  • Xilin Gu

    (University of California)

  • Jason K. Sello

    (University of California)

  • Richard D. Vierstra

    (Washington University in St. Louis)

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.

Suggested Citation

  • Hana Zand Karimi & Kuo-En Chen & Marilee Karinshak & Xilin Gu & Jason K. Sello & Richard D. Vierstra, 2025. "Proteasomes accumulate in the plant apoplast where they participate in microbe-associated molecular pattern (MAMP)-triggered pathogen defense," Nature Communications, Nature, vol. 16(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56594-3
    DOI: 10.1038/s41467-025-56594-3
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-56594-3
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-56594-3?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Michael Groll & Barbara Schellenberg & André S. Bachmann & Crystal R. Archer & Robert Huber & Tracy K. Powell & Steven Lindow & Markus Kaiser & Robert Dudler, 2008. "A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism," Nature, Nature, vol. 452(7188), pages 755-758, April.
    2. Koji Yonekura & Saori Maki-Yonekura & Keiichi Namba, 2003. "Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy," Nature, Nature, vol. 424(6949), pages 643-650, August.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. William R Taylor & Teige R S Matthews-Palmer & Morgan Beeby, 2016. "Molecular Models for the Core Components of the Flagellar Type-III Secretion Complex," PLOS ONE, Public Library of Science, vol. 11(11), pages 1-33, November.
    2. Jessie Lynda Fields & Hua Zhang & Nathan F. Bellis & Holly A. Petersen & Sajal K. Halder & Shane T. Rich-New & Mart Krupovic & Hui Wu & Fengbin Wang, 2024. "Structural diversity and clustering of bacterial flagellar outer domains," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    3. Manuel Halte & Ekaterina P. Andrianova & Christian Goosmann & Fabienne F. V. Chevance & Kelly T. Hughes & Igor B. Zhulin & Marc Erhardt, 2024. "FlhE functions as a chaperone to prevent formation of periplasmic flagella in Gram-negative bacteria," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    4. Nicholas M Thomson & Josie L Ferreira & Teige R Matthews-Palmer & Morgan Beeby & Mark J Pallen, 2018. "Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria," PLOS ONE, Public Library of Science, vol. 13(11), pages 1-12, November.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56594-3. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.