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Membrane-cytoskeletal crosstalk mediated by myosin-I regulates adhesion turnover during phagocytosis

Author

Listed:
  • Sarah R. Barger

    (State University of New York Upstate Medical University)

  • Nicholas S. Reilly

    (University of Rochester)

  • Maria S. Shutova

    (University of Pennsylvania)

  • Qingsen Li

    (FIRC Institute of Molecular Oncology)

  • Paolo Maiuri

    (FIRC Institute of Molecular Oncology)

  • John M. Heddleston

    (Howard Hughes Medical Institute Janelia Research Campus)

  • Mark S. Mooseker

    (Yale University)

  • Richard A. Flavell

    (Yale University School of Medicine
    Yale University)

  • Tatyana Svitkina

    (University of Pennsylvania)

  • Patrick W. Oakes

    (University of Rochester
    University of Rochester)

  • Mira Krendel

    (State University of New York Upstate Medical University)

  • Nils C. Gauthier

    (FIRC Institute of Molecular Oncology)

Abstract

Phagocytosis of invading pathogens or cellular debris requires a dramatic change in cell shape driven by actin polymerization. For antibody-covered targets, phagocytosis is thought to proceed through the sequential engagement of Fc-receptors on the phagocyte with antibodies on the target surface, leading to the extension and closure of the phagocytic cup around the target. We find that two actin-dependent molecular motors, class 1 myosins myosin 1e and myosin 1f, are specifically localized to Fc-receptor adhesions and required for efficient phagocytosis of antibody-opsonized targets. Using primary macrophages lacking both myosin 1e and myosin 1f, we find that without the actin-membrane linkage mediated by these myosins, the organization of individual adhesions is compromised, leading to excessive actin polymerization, slower adhesion turnover, and deficient phagocytic internalization. This work identifies a role for class 1 myosins in coordinated adhesion turnover during phagocytosis and supports a mechanism involving membrane-cytoskeletal crosstalk for phagocytic cup closure.

Suggested Citation

  • Sarah R. Barger & Nicholas S. Reilly & Maria S. Shutova & Qingsen Li & Paolo Maiuri & John M. Heddleston & Mark S. Mooseker & Richard A. Flavell & Tatyana Svitkina & Patrick W. Oakes & Mira Krendel & , 2019. "Membrane-cytoskeletal crosstalk mediated by myosin-I regulates adhesion turnover during phagocytosis," Nature Communications, Nature, vol. 10(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09104-1
    DOI: 10.1038/s41467-019-09104-1
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    Cited by:

    1. Kay Oliver Schink & Kia Wee Tan & Hélène Spangenberg & Domenica Martorana & Marte Sneeggen & Virginie Stévenin & Jost Enninga & Coen Campsteijn & Camilla Raiborg & Harald Stenmark, 2021. "The phosphoinositide coincidence detector Phafin2 promotes macropinocytosis by coordinating actin organisation at forming macropinosomes," Nature Communications, Nature, vol. 12(1), pages 1-17, December.
    2. Tatsat Banerjee & Satomi Matsuoka & Debojyoti Biswas & Yuchuan Miao & Dhiman Sankar Pal & Yoichiro Kamimura & Masahiro Ueda & Peter N. Devreotes & Pablo A. Iglesias, 2023. "A dynamic partitioning mechanism polarizes membrane protein distribution," Nature Communications, Nature, vol. 14(1), pages 1-24, December.

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