However, the structures and functional diversities of the mammalian F-BAR family have not been elucidated. Recently, research has started to reveal potential functions for F-BAR proteins. F-BAR domain family is a member of the Bin/Amphiphysin/Rvs (BAR) domain superfamily which also includes the N-terminal amphipathic helix BAR (N-BAR) domain family and inverse BAR (I-BAR) domain family. F-BAR proteins are membrane-associated proteins and regulate membrane curvature via binding to cell membrane phospholipids. Recently, a group of proteins named Fes/CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domain family has emerged as the critical coordinators that regulate membrane curvature. The ability of cell membrane to achieve these dynamics is heavily determined by the collaboration between actin cytoskeleton and membrane-interacting proteins. 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.Ĭell membrane curvature is a micro morphological change involved in many important cellular processes including endocytosis, phagocytosis, exocytosis, angiogenisis, and migration. We further summarize F-BAR protein expression and mutation changes observed in various diseases and developmental disorders. These cellular functions play important roles in many physiological and pathophysiological processes. 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. 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 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. The pathophysiological role of F-BAR protein is unknown. However, the molecular basis in membrane structure regulation and the biological functions of F-BAR protein are unclear. 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. 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. Eukaryotic cell membrane dynamics change in curvature during physiological and pathological processes.
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