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; Shiro Suetsugu

doi:10.1038/s41467-019-12738-w

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, Shiro Suetsugu

Department of Molecular and Structural Biology

Research output: Contribution to journal › Article

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.

Original language	English
Article number	4763
Journal	Nature communications
Volume	10
Issue number	1
DOIs	https://doi.org/10.1038/s41467-019-12738-w
Publication status	Published - Dec 1 2019

All Science Journal Classification (ASJC) codes

Chemistry(all)
Biochemistry, Genetics and Molecular Biology(all)
Physics and Astronomy(all)

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Hanawa-Suetsugu, K., Itoh, Y., Ab Fatah, M., Nishimura, T., Takemura, K., Takeshita, K., Kubota, S., Miyazaki, N., Wan Mohamad Noor, W. N. I., Inaba, T., Nguyen, N. T. H., Hamada-Nakahara, S., Oono-Yakura, K., Tachikawa, M., Iwasaki, K., Kohda, D., Yamamoto, M., Kitao, A., Shimada, A., & Suetsugu, S. (2019). Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7. Nature communications, 10(1), [4763]. https://doi.org/10.1038/s41467-019-12738-w

Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7. / Hanawa-Suetsugu, Kyoko; Itoh, Yuzuru; Ab Fatah, Maisarah; Nishimura, Tamako; Takemura, Kazuhiro; Takeshita, Kohei; Kubota, Satoru; Miyazaki, Naoyuki; Wan Mohamad Noor, Wan Nurul Izzati; Inaba, Takehiko; Nguyen, Nhung Thi Hong; Hamada-Nakahara, Sayaka; Oono-Yakura, Kayoko; Tachikawa, Masashi; Iwasaki, Kenji; Kohda, Daisuke; Yamamoto, Masaki; Kitao, Akio; Shimada, Atsushi; Suetsugu, Shiro.

In: Nature communications, Vol. 10, No. 1, 4763, 01.12.2019.

Research output: Contribution to journal › Article

Hanawa-Suetsugu, K, Itoh, Y, Ab Fatah, M, Nishimura, T, Takemura, K, Takeshita, K, Kubota, S, Miyazaki, N, Wan Mohamad Noor, WNI, Inaba, T, Nguyen, NTH, Hamada-Nakahara, S, Oono-Yakura, K, Tachikawa, M, Iwasaki, K, Kohda, D, Yamamoto, M, Kitao, A, Shimada, A & Suetsugu, S 2019, 'Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7', Nature communications, vol. 10, no. 1, 4763. https://doi.org/10.1038/s41467-019-12738-w

Hanawa-Suetsugu, Kyoko ; Itoh, Yuzuru ; Ab Fatah, Maisarah ; Nishimura, Tamako ; Takemura, Kazuhiro ; Takeshita, Kohei ; Kubota, Satoru ; Miyazaki, Naoyuki ; Wan Mohamad Noor, Wan Nurul Izzati ; Inaba, Takehiko ; Nguyen, Nhung Thi Hong ; Hamada-Nakahara, Sayaka ; Oono-Yakura, Kayoko ; Tachikawa, Masashi ; Iwasaki, Kenji ; Kohda, Daisuke ; Yamamoto, Masaki ; Kitao, Akio ; Shimada, Atsushi ; Suetsugu, Shiro. / Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7. In: Nature communications. 2019 ; Vol. 10, No. 1.

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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.",

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AU - Hamada-Nakahara, Sayaka

AU - Oono-Yakura, Kayoko

AU - Tachikawa, Masashi

AU - Iwasaki, Kenji

AU - Kohda, Daisuke

AU - Yamamoto, Masaki

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AU - Shimada, Atsushi

AU - Suetsugu, Shiro

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N2 - 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.

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