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Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7

Author

Listed:
  • Kyoko Hanawa-Suetsugu

    (Nara Institute of Science and Technology)

  • Yuzuru Itoh

    (University of Tokyo
    Stockholm University)

  • Maisarah Ab Fatah

    (Nara Institute of Science and Technology)

  • Tamako Nishimura

    (Nara Institute of Science and Technology)

  • Kazuhiro Takemura

    (Tokyo Institute of Technology)

  • Kohei Takeshita

    (RIKEN SPring-8 Center)

  • Satoru Kubota

    (Nara Institute of Science and Technology)

  • Naoyuki Miyazaki

    (Osaka University)

  • Wan Nurul Izzati Wan Mohamad Noor

    (Nara Institute of Science and Technology)

  • Takehiko Inaba

    (Nara Institute of Science and Technology)

  • Nhung Thi Hong Nguyen

    (Nara Institute of Science and Technology)

  • Sayaka Hamada-Nakahara

    (University of Tokyo)

  • Kayoko Oono-Yakura

    (Nara Institute of Science and Technology)

  • Masashi Tachikawa

    (RIKEN)

  • Kenji Iwasaki

    (Osaka University
    University of Tsukuba)

  • Daisuke Kohda

    (RIKEN SPring-8 Center
    Kyushu University)

  • Masaki Yamamoto

    (RIKEN SPring-8 Center)

  • Akio Kitao

    (Tokyo Institute of Technology)

  • Atsushi Shimada

    (RIKEN SPring-8 Center
    Kyushu University)

  • Shiro Suetsugu

    (Nara Institute of Science and Technology)

Abstract

Phagocytosis is a cellular process for internalization of micron-sized large particles including pathogens. The Bin-Amphiphysin-Rvs167 (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, impose specific morphologies on lipid membranes. Most BAR domain proteins are thought to form membrane invaginations or protrusions by assembling into helical submicron-diameter filaments, such as on clathrin-coated pits, caveolae, and filopodia. However, the mechanism by which BAR domain proteins assemble into micron-scale phagocytic cups was unclear. Here, we show that the two-dimensional sheet-like assembly of Growth Arrest-Specific 7 (GAS7) plays a critical role in phagocytic cup formation in macrophages. GAS7 has the F-BAR domain that possesses unique hydrophilic loops for two-dimensional sheet formation on flat membranes. Super-resolution microscopy reveals the similar assemblies of GAS7 on phagocytic cups and liposomes. The mutations of the loops abolishes both the membrane localization of GAS7 and phagocytosis. Thus, the sheet-like assembly of GAS7 plays a significant role in phagocytosis.

Suggested Citation

  • Kyoko Hanawa-Suetsugu & Yuzuru Itoh & Maisarah Ab Fatah & Tamako Nishimura & Kazuhiro Takemura & Kohei Takeshita & Satoru Kubota & Naoyuki Miyazaki & Wan Nurul Izzati Wan Mohamad Noor & Takehiko Inaba, 2019. "Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12738-w
    DOI: 10.1038/s41467-019-12738-w
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