ABSTRACT
Proteins that belong to the BAR (Bin, Amphiphysin, RVS) domain superfamily are alpha-helical bilayer-binding modules that have evolved to induce or stabilize membrane curvature during cellular events like endocytosis, cell division and organelle biogenesis. Within the superfam ily, a subset o f proteins possessing F-BAR (Fes/CIP4 homology-BAR) domains play key roles in membrane remodeling and loss-of-function mutations in genes coding for F-BAR proteins are associated with human diseases. Here, we review how F-BAR domains compare structurally with related members o f the BAR domain superfamily and discuss the proposed mechanisms underlying their membrane-molding activity and regulation. We end by highlighting the functional properties o f select F-BAR domains that were elucidated by electron cryo-microscopy and 3D reconstruction o f these modules while bound to flat and curved membranes.
