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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
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    References listed on IDEAS

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    1. 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.
    2. 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.
    3. 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.
    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.
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    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.

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