IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-15327-4.html
   My bibliography  Save this article

Anisotropic ESCRT-III architecture governs helical membrane tube formation

Author

Listed:
  • Joachim Moser von Filseck

    (University of Geneva)

  • Luca Barberi

    (Université Paris-Sud, Université Paris-Saclay
    University of Geneva)

  • Nathaniel Talledge

    (University of California, San Francisco
    California Institute for Quantitative Biosciences
    University of Utah
    University of Minnesota-Twin Cities)

  • Isabel E. Johnson

    (University of California, San Francisco
    California Institute for Quantitative Biosciences)

  • Adam Frost

    (University of California, San Francisco
    California Institute for Quantitative Biosciences
    University of Utah
    Chan Zuckerberg Biohub)

  • Martin Lenz

    (Université Paris-Sud, Université Paris-Saclay
    Laboratoire de Physique et Mécanique des Milieux Hétérogènes, UMR 7636, CNRS, ESPCI Paris, PSL Research University, Université Paris Diderot, Sorbonne Université)

  • Aurélien Roux

    (University of Geneva
    Swiss National Centre for Competence in Research Programme Chemical Biology)

Abstract

ESCRT-III proteins assemble into ubiquitous membrane-remodeling polymers during many cellular processes. Here we describe the structure of helical membrane tubes that are scaffolded by bundled ESCRT-III filaments. Cryo-ET reveals how the shape of the helical membrane tube arises from the assembly of two distinct bundles of helical filaments that have the same helical path but bind the membrane with different interfaces. Higher-resolution cryo-EM of filaments bound to helical bicelles confirms that ESCRT-III filaments can interact with the membrane through a previously undescribed interface. Mathematical modeling demonstrates that the interface described above is key to the mechanical stability of helical membrane tubes and helps infer the rigidity of the described protein filaments. Altogether, our results suggest that the interactions between ESCRT-III filaments and the membrane could proceed through multiple interfaces, to provide assembly on membranes with various shapes, or adapt the orientation of the filaments towards the membrane during membrane remodeling.

Suggested Citation

  • Joachim Moser von Filseck & Luca Barberi & Nathaniel Talledge & Isabel E. Johnson & Adam Frost & Martin Lenz & Aurélien Roux, 2020. "Anisotropic ESCRT-III architecture governs helical membrane tube formation," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15327-4
    DOI: 10.1038/s41467-020-15327-4
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-15327-4
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-020-15327-4?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
    ---><---

    Citations

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


    Cited by:

    1. Nebojsa Jukic & Alma P. Perrino & Frédéric Humbert & Aurélien Roux & Simon Scheuring, 2022. "Snf7 spirals sense and alter membrane curvature," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    2. Chao Su & Marta Rodriguez-Franco & Beatrice Lace & Nils Nebel & Casandra Hernandez-Reyes & Pengbo Liang & Eija Schulze & Evgeny V. Mymrikov & Nikolas M. Gross & Julian Knerr & Hong Wang & Lina Siuksta, 2023. "Stabilization of membrane topologies by proteinaceous remorin scaffolds," Nature Communications, Nature, vol. 14(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:11:y:2020:i:1:d:10.1038_s41467-020-15327-4. 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.

    We have no bibliographic references for this item. You can help adding them by using 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.