ReviewJournal of hematology & oncology2015
F-BAR family proteins, emerging regulators for cell membrane dynamic changes-from structure to human diseases.
Review in Journal of hematology & oncology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 85 citations in OpenAlex.
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- Plasma membrane invaginations and their diverse cellular functions.BMC biology · 2026Review
- Membrane Curvature Activates Src kinase and Promotes Metastatic Cancer Cell Survival.bioRxiv : the preprint server for biology · 2026Article
- Membrane curvature initiates Cdc42-FBP17-N-WASP clustering and actin nucleation.The EMBO journal · 2026Article
- Targeting of Cdc42-Interacting Protein 4-Calcineurin Signalosomes Improves Cardiac Structure and Function After Myocardial Infarction.Journal of the American Heart Association · 2026Article
- Phase separation drives cortical enrichment of the F-BAR proteins Rga7 and Rga8 to maintain cell integrity.Cellular and molecular life sciences : CMLS · 2025Article
- Diagnostic significance of cardiac bridging integrator 1 score in hospitalized patients with heart failure with preserved ejection fraction and its assessment of prognostic value for major adverse cardiac events.BMC cardiovascular disorders · 2025Article
- WAVE complex forms linear arrays at negative membrane curvature to instruct lamellipodia formation.The Journal of cell biology · 2025Article
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- Zika Virus Infection Modulates Extracellular Vesicle Biogenesis and Morphology in Human Umbilical Cord Endothelial Cells: A Proteomic and Microscopic Analysis.Microorganisms · 2025Article
- Cellular Signaling at the Nano-Bio Interface: Spotlighting Membrane Curvature.Annual review of physical chemistry · 2025Review
- Genetic factors associated with erectile dysfunction- mendelian randomisation analysis.American journal of clinical and experimental urology · 2025Article
- Article
- Molecular Dynamics Reveal Key Steps in BAR-Related Membrane Remodeling.Pathogens (Basel, Switzerland) · 2024Article
- Distinct Bin/Amphiphysin/Rvs (BAR) family proteins may assemble on the same tubule to regulate membrane organizationHeliyon · 2024Article
- Comprehensive Analyses of the Effects of the Small-Molecule Inhibitor of the UHM Domain in the Splicing FactorResearch square · 2024Article
- Interrupting an IFN-γ-dependent feedback loop in the syndrome of pyogenic arthritis with pyoderma gangrenosum and acne.Annals of the rheumatic diseases · 2024Article
- Identification of novel hypermethylated or hypomethylated CpG sites and genes associated with anthracycline-induced cardiomyopathy.Scientific reports · 2023Article
- Genomic structural variation: A complex but important driver of human evolution.American journal of biological anthropology · 2023Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Eukaryotic cell membrane dynamics change in curvature during physiological and pathological processes. In the past ten years, a novel protein family, Fes/CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domain proteins, has been identified to be the most important coordinators in membrane curvature regulation. The F-BAR domain family is a member of the Bin/Amphiphysin/Rvs (BAR) domain superfamily that is associated with dynamic changes in cell membrane. However, the molecular basis in membrane structure regulation and the biological functions of F-BAR protein are unclear. The pathophysiological role of F-BAR protein is unknown. This review summarizes the current understanding of structure and function in the BAR domain superfamily, classifies F-BAR family proteins into nine subfamilies based on domain structure, and characterizes F-BAR protein structure, domain interaction, and functional relevance. In general, F-BAR protein binds to cell membrane via F-BAR domain association with membrane phospholipids and initiates membrane curvature and scission via Src homology-3 (SH3) domain interaction with its partner proteins. This process causes membrane dynamic changes and leads to seven important cellular biological functions, which include endocytosis, phagocytosis, filopodium, lamellipodium, cytokinesis, adhesion, and podosome formation, via distinct signaling pathways determined by specific domain-binding partners. These cellular functions play important roles in many physiological and pathophysiological processes. We further summarize F-BAR protein expression and mutation changes observed in various diseases and developmental disorders. Considering the structure feature and functional implication of F-BAR proteins, we anticipate that F-BAR proteins modulate physiological and pathophysiological processes via transferring extracellular materials, regulating cell trafficking and mobility, presenting antigens, mediating extracellular matrix degradation, and transmitting signaling for cell proliferation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.