Unknown

Dataset Information

0

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


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.

SUBMITTER: Hanawa-Suetsugu K 

PROVIDER: S-EPMC6802115 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications


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 prote  ...[more]

Similar Datasets

| S-EPMC6660589 | biostudies-literature
| S-EPMC3527510 | biostudies-literature
| S-EPMC6062498 | biostudies-literature
| S-EPMC3665323 | biostudies-literature
| S-EPMC7540408 | biostudies-literature
| S-EPMC5830438 | biostudies-other
2018-10-18 | PXD010150 | Pride
| S-EPMC168943 | biostudies-literature
| S-EPMC2722316 | biostudies-literature
| S-EPMC5633016 | biostudies-literature