Details

Autor(en) / Beteiligte

• 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

Titel

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

Ist Teil von

• Nature communications, 2019-10, Vol.10 (1), p.4763-13, Article 4763

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2019

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.