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 | |
| Publication status | Published - Dec 1 2019 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)
Cite this
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
}
TY - JOUR
T1 - Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7
AU - Hanawa-Suetsugu, Kyoko
AU - Itoh, Yuzuru
AU - Ab Fatah, Maisarah
AU - Nishimura, Tamako
AU - Takemura, Kazuhiro
AU - Takeshita, Kohei
AU - Kubota, Satoru
AU - Miyazaki, Naoyuki
AU - Wan Mohamad Noor, Wan Nurul Izzati
AU - Inaba, Takehiko
AU - Nguyen, Nhung Thi Hong
AU - Hamada-Nakahara, Sayaka
AU - Oono-Yakura, Kayoko
AU - Tachikawa, Masashi
AU - Iwasaki, Kenji
AU - Kohda, Daisuke
AU - Yamamoto, Masaki
AU - Kitao, Akio
AU - Shimada, Atsushi
AU - Suetsugu, Shiro
PY - 2019/12/1
Y1 - 2019/12/1
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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85073511723&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85073511723&partnerID=8YFLogxK
U2 - 10.1038/s41467-019-12738-w
DO - 10.1038/s41467-019-12738-w
M3 - Article
C2 - 31628328
AN - SCOPUS:85073511723
VL - 10
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 4763
ER -