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

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, Nhung Thi Hong Nguyen, Sayaka Hamada-Nakahara, Kayoko Oono-Yakura, Masashi Tachikawa, Kenji Iwasaki, Daisuke Kohda, Masaki Yamamoto, Akio Kitao, Atsushi Shimada () and Shiro Suetsugu ()
Additional contact information
Kyoko Hanawa-Suetsugu: Nara Institute of Science and Technology
Yuzuru Itoh: University of Tokyo
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
Daisuke Kohda: RIKEN SPring-8 Center
Masaki Yamamoto: RIKEN SPring-8 Center
Akio Kitao: Tokyo Institute of Technology
Atsushi Shimada: RIKEN SPring-8 Center
Shiro Suetsugu: Nara Institute of Science and Technology

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-12738-w

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