IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-32109-2.html
   My bibliography  Save this article

Phosphatidylinositol-4-phosphate controls autophagosome formation in Arabidopsis thaliana

Author

Listed:
  • Rodrigo Enrique Gomez

    (Univ. Bordeaux)

  • Clément Chambaud

    (Univ. Bordeaux)

  • Josselin Lupette

    (Univ. Bordeaux)

  • Julie Castets

    (Univ. Bordeaux)

  • Stéphanie Pascal

    (Univ. Bordeaux)

  • Lysiane Brocard

    (Univ. Bordeaux)

  • Lise Noack

    (Univ. Lyon, ENS de Lyon, CNRS, INRAE)

  • Yvon Jaillais

    (Univ. Lyon, ENS de Lyon, CNRS, INRAE)

  • Jérôme Joubès

    (Univ. Bordeaux)

  • Amélie Bernard

    (Univ. Bordeaux)

Abstract

Autophagy is an intracellular degradation mechanism critical for plant acclimation to environmental stresses. Central to autophagy is the formation of specialized vesicles, the autophagosomes, which target and deliver cargo to the lytic vacuole. How autophagosomes form in plant cells remains poorly understood. Here, we uncover the importance of the lipid phosphatidylinositol-4-phosphate in autophagy using pharmacological and genetical approaches. Combining biochemical and live-microscopy analyses, we show that PI4K activity is required for early stages of autophagosome formation. Further, our results show that the plasma membrane-localized PI4Kα1 is involved in autophagy and that a substantial portion of autophagy structures are found in proximity to the PI4P-enriched plasma membrane. Together, our study unravels critical insights into the molecular determinants of autophagy, proposing a model whereby the plasma membrane provides PI4P to support the proper assembly and expansion of the phagophore thus governing autophagosome formation in Arabidopsis.

Suggested Citation

  • Rodrigo Enrique Gomez & Clément Chambaud & Josselin Lupette & Julie Castets & Stéphanie Pascal & Lysiane Brocard & Lise Noack & Yvon Jaillais & Jérôme Joubès & Amélie Bernard, 2022. "Phosphatidylinositol-4-phosphate controls autophagosome formation in Arabidopsis thaliana," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32109-2
    DOI: 10.1038/s41467-022-32109-2
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-32109-2
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-022-32109-2?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. Yoko Ito & Nicolas Esnay & Matthieu Pierre Platre & Valérie Wattelet-Boyer & Lise C. Noack & Louise Fougère & Wilhelm Menzel & Stéphane Claverol & Laetitia Fouillen & Patrick Moreau & Yvon Jaillais & , 2021. "Sphingolipids mediate polar sorting of PIN2 through phosphoinositide consumption at the trans-Golgi network," Nature Communications, Nature, vol. 12(1), pages 1-18, December.
    2. Pengwei Wang & Roman Pleskot & Jingze Zang & Joanna Winkler & Jie Wang & Klaas Yperman & Tong Zhang & Kun Wang & Jinli Gong & Yajie Guan & Christine Richardson & Patrick Duckney & Michael Vandorpe & E, 2019. "Plant AtEH/Pan1 proteins drive autophagosome formation at ER-PM contact sites with actin and endocytic machinery," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
    Full references (including those not matched with items on IDEAS)

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Lin-lin Zhao & Ru Chen & Ziyu Bai & Junyi Liu & Yuhao Zhang & Yicheng Zhong & Meng-xiang Sun & Peng Zhao, 2024. "Autophagy-mediated degradation of integumentary tapetum is critical for embryo pattern formation," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

    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. Lin-lin Zhao & Ru Chen & Ziyu Bai & Junyi Liu & Yuhao Zhang & Yicheng Zhong & Meng-xiang Sun & Peng Zhao, 2024. "Autophagy-mediated degradation of integumentary tapetum is critical for embryo pattern formation," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Tong Zhang & Yifan Li & Chengyang Li & Jingze Zang & Erlin Gao & Johan T. Kroon & Xiaolu Qu & Patrick J. Hussey & Pengwei Wang, 2023. "Exo84c interacts with VAP27 to regulate exocytotic compartment degradation and stigma senescence," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Luciana Renna & Giovanni Stefano & Maria Paola Puggioni & Sang-Jin Kim & Anastasiya Lavell & John E. Froehlich & Graham Burkart & Stefano Mancuso & Christoph Benning & Federica Brandizzi, 2024. "ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    4. Timothy J. Hawkins & Michaela Kopischke & Patrick J. Duckney & Katarzyna Rybak & David A. Mentlak & Johan T. M. Kroon & Mai Thu Bui & A. Christine Richardson & Mary Casey & Agnieszka Alexander & Geert, 2023. "NET4 and RabG3 link actin to the tonoplast and facilitate cytoskeletal remodelling during stomatal immunity," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    5. José Cerca & Bent Petersen & José Miguel Lazaro-Guevara & Angel Rivera-Colón & Siri Birkeland & Joel Vizueta & Siyu Li & Qionghou Li & João Loureiro & Chatchai Kosawang & Patricia Jaramillo Díaz & Gon, 2022. "The genomic basis of the plant island syndrome in Darwin’s giant daisies," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    6. Chengyang Li & Patrick Duckney & Tong Zhang & Yanshu Fu & Xin Li & Johan Kroon & Geert Jaeger & Yunjiang Cheng & Patrick J. Hussey & Pengwei Wang, 2022. "TraB family proteins are components of ER-mitochondrial contact sites and regulate ER-mitochondrial interactions and mitophagy," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

    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:13:y:2022:i:1:d:10.1038_s41467-022-32109-2. 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.