IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-31207-5.html
   My bibliography  Save this article

Branched actin networks are organized for asymmetric force production during clathrin-mediated endocytosis in mammalian cells

Author

Listed:
  • Meiyan Jin

    (University of California)

  • Cyna Shirazinejad

    (University of California
    University of California Berkeley)

  • Bowen Wang

    (University of California)

  • Amy Yan

    (University of California)

  • Johannes Schöneberg

    (University of California
    University of California)

  • Srigokul Upadhyayula

    (University of California
    Chan Zuckerberg Biohub)

  • Ke Xu

    (University of California)

  • David G. Drubin

    (University of California)

Abstract

Actin assembly facilitates vesicle formation in several trafficking pathways, including clathrin-mediated endocytosis (CME). Interestingly, actin does not assemble at all CME sites in mammalian cells. How actin networks are organized with respect to mammalian CME sites and how assembly forces are harnessed, are not fully understood. Here, branched actin network geometry at CME sites was analyzed using three different advanced imaging approaches. When endocytic dynamics of unperturbed CME sites are compared, sites with actin assembly show a distinct signature, a delay between completion of coat expansion and vesicle scission, indicating that actin assembly occurs preferentially at stalled CME sites. In addition, N-WASP and the Arp2/3 complex are recruited to one side of CME sites, where they are positioned to stimulate asymmetric actin assembly and force production. We propose that actin assembles preferentially at stalled CME sites where it pulls vesicles into the cell asymmetrically, much as a bottle opener pulls off a bottle cap.

Suggested Citation

  • Meiyan Jin & Cyna Shirazinejad & Bowen Wang & Amy Yan & Johannes Schöneberg & Srigokul Upadhyayula & Ke Xu & David G. Drubin, 2022. "Branched actin networks are organized for asymmetric force production during clathrin-mediated endocytosis in mammalian cells," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31207-5
    DOI: 10.1038/s41467-022-31207-5
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-31207-5
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-31207-5?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. Dinah Loerke & Marcel Mettlen & Defne Yarar & Khuloud Jaqaman & Henry Jaqaman & Gaudenz Danuser & Sandra L Schmid, 2009. "Cargo and Dynamin Regulate Clathrin-Coated Pit Maturation," PLOS Biology, Public Library of Science, vol. 7(3), pages 1-12, March.
    2. Michal Wojcik & Margaret Hauser & Wan Li & Seonah Moon & Ke Xu, 2015. "Graphene-enabled electron microscopy and correlated super-resolution microscopy of wet cells," Nature Communications, Nature, vol. 6(1), pages 1-6, November.
    3. Delia Bucher & Felix Frey & Kem A. Sochacki & Susann Kummer & Jan-Philip Bergeest & William J. Godinez & Hans-Georg Kräusslich & Karl Rohr & Justin W. Taraska & Ulrich S. Schwarz & Steeve Boulant, 2018. "Clathrin-adaptor ratio and membrane tension regulate the flat-to-curved transition of the clathrin coat during endocytosis," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    4. Mohammed Saleem & Sandrine Morlot & Annika Hohendahl & John Manzi & Martin Lenz & Aurélien Roux, 2015. "A balance between membrane elasticity and polymerization energy sets the shape of spherical clathrin coats," Nature Communications, Nature, vol. 6(1), pages 1-10, May.
    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. Ling-Gang Wu & Chung Yu Chan, 2024. "Membrane transformations of fusion and budding," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Yiming Yu & Shige H. Yoshimura, 2023. "Self-assembly of CIP4 drives actin-mediated asymmetric pit-closing in clathrin-mediated endocytosis," Nature Communications, Nature, vol. 14(1), pages 1-15, 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. Tomasz J. Nawara & Yancey D. Williams & Tejeshwar C. Rao & Yuesong Hu & Elizabeth Sztul & Khalid Salaita & Alexa L. Mattheyses, 2022. "Imaging vesicle formation dynamics supports the flexible model of clathrin-mediated endocytosis," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Kazuki Obashi & Kem A. Sochacki & Marie-Paule Strub & Justin W. Taraska, 2023. "A conformational switch in clathrin light chain regulates lattice structure and endocytosis at the plasma membrane of mammalian cells," Nature Communications, Nature, vol. 14(1), pages 1-15, 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_s41467-022-31207-5. 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.