ArticleNature communications2019
Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- IL-33/ST2 Signaling and Microglial Functional-State Transitions After Spinal Cord Injury: Direct Evidence and Mechanistic Hypotheses.International journal of molecular sciences · 2026Review
- PHF20 stabilizes the GAS7-F-actin axis to drive DNA damage repair and chemoresistance in cutaneous squamous cell carcinoma.Cell death & disease · 2026Article
- WAVE complex forms linear arrays at negative membrane curvature to instruct lamellipodia formation.The Journal of cell biology · 2025Article
- Machine Learning-Directed Conversion of Glioblastoma Cells to Dendritic Cell-Like Antigen-Presenting Cells as Cancer Immunotherapy.Cancer immunology research · 2024Article
- MSCs mediate long-term efficacy in a Crohn's disease model by sustained anti-inflammatory macrophage programming via efferocytosis.NPJ Regenerative medicine · 2024Article
- Small GTPase Cdc42, WASP, and scaffold proteins for higher-order assembly of the F-BAR domain protein.Science advances · 2023Article
- Mechanisms Underlying the Suppression of IL-1β Expression by Magnesium Hydroxide Nanoparticles.Biomedicines · 2023Article
- Gas7 Is a Novel Dendritic Spine Initiation Factor.eNeuro · 2023Article
- Actin Filaments Couple the Protrusive Tips to the Nucleus through the I-BAR Domain Protein IRSp53 during the Migration of Cells on 1D Fibers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Theoretical model of membrane protrusions driven by curved active proteins.Frontiers in molecular biosciences · 2023Article
- A theoretical model of efficient phagocytosis driven by curved membrane proteins and active cytoskeleton forces.Soft matter · 2022Article
- Single cell transcriptomics of Atlantic salmon (Frontiers in immunology · 2022Article
- Cell membrane coating integrity affects the internalization mechanism of biomimetic nanoparticles.Nature communications · 2021Article
- Dendritic Spine Initiation in Brain Development, Learning and Diseases and Impact of BAR-Domain Proteins.Cells · 2021Review
- Phosphorylation in the intrinsically disordered region of F-BAR protein Imp2 regulates its contractile ring recruitment.Journal of cell science · 2021Article
- The state of F-BAR domains as membrane-bound oligomeric platforms.Trends in cell biology · 2021Review
- GAS7 Deficiency Promotes Metastasis in MYCN-Driven Neuroblastoma.Cancer research · 2021Article
- Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.Cell reports · 2020Article
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Authors and funding
20 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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