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

Autor: Takehiko Inaba, Kenji Iwasaki, Shiro Suetsugu, Naoyuki Miyazaki, Kyoko Hanawa-Suetsugu, Maisarah Ab Fatah, Akio Kitao, Yuzuru Itoh, Kazuhiro Takemura, Daisuke Kohda, Kohei Takeshita, Atsushi Shimada, Nhung Thi Hong Nguyen, Wan Nurul Izzati Wan Mohamad Noor, Sayaka Hamada-Nakahara, Masashi Tachikawa, Masaki Yamamoto, Tamako Nishimura, Kayoko Oono-Yakura, Satoru Kubota
Rok vydání: 2018
Předmět:
0301 basic medicine
Phagocytic cup
Models
Molecular
genetic structures
Phagocytosis
Science
Protein domain
General Physics and Astronomy
Nerve Tissue Proteins
General Biochemistry
Genetics and Molecular Biology
Article
03 medical and health sciences
Membrane Lipids
Mice
0302 clinical medicine
Protein Domains
Caveolae
BAR domain
Animals
Humans
Protein Isoforms
Cell migration
Amino Acid Sequence
Super-resolution microscopy
lcsh:Science
X-ray crystallography
Multidisciplinary
Sequence Homology
Amino Acid
Chemistry
Macrophages
Cell Membrane
Membrane structure and assembly
General Chemistry
Antimicrobial responses
Microscopy
Electron
030104 developmental biology
Membrane
RAW 264.7 Cells
Microscopy
Fluorescence
Amphiphysin
Mutation
Biophysics
lcsh:Q
Filopodia
030217 neurology & neurosurgery
HeLa Cells
Zdroj: Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
ISSN: 2041-1723
Popis: 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.
The Bin/Amphiphysin/Rvs167 (BAR) domain superfamily, which includes FCH-BAR (F-BAR) domain proteins are membrane-sculpting proteins. Here the authors combine a range of techniques and show that the F-BAR domain of growth-arrest specific protein 7 (GAS7) forms two-dimensional sheets on flat membranes and that these oligomeric assemblies of GAS7 are required for the formation of phagocytic cups in macrophages.
Databáze: OpenAIRE
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