『堀河百首肝要抄』について : 編者と注釈と

application/pdf女子大文学. 國文篇 : 大阪女子大學紀要. 2004, 55, p.25-38departmental bulletin pape

液体シンチレーションカウンター TRI-CARB 2910TR の紹介《forum in FORUM》

textapplication/pdfdepartmental bulletin pape

Studies of CP Violation in B→J/ψK* Decays

journal articl

最高裁違憲破棄判例の手続問題序説

2008-06-30河野正憲教授退職記念論文集departmental bulletin pape

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

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.journal articl