Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7.
Amino Acid Sequence
Animals
Cell Membrane
/ chemistry
HeLa Cells
Humans
Macrophages
/ metabolism
Membrane Lipids
/ chemistry
Mice
Microscopy, Electron
Microscopy, Fluorescence
Models, Molecular
Mutation
Nerve Tissue Proteins
/ chemistry
Phagocytosis
Protein Domains
Protein Isoforms
/ chemistry
RAW 264.7 Cells
Sequence Homology, Amino Acid
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 10 2019
18 10 2019
Historique:
received:
21
11
2018
accepted:
26
09
2019
entrez:
20
10
2019
pubmed:
20
10
2019
medline:
25
1
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31628328
doi: 10.1038/s41467-019-12738-w
pii: 10.1038/s41467-019-12738-w
pmc: PMC6802115
doi:
Substances chimiques
Gas7 protein, mouse
0
Membrane Lipids
0
Nerve Tissue Proteins
0
Protein Isoforms
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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