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 superfamily, a subset of 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 of the BAR domain superfamily and discuss the proposed mechanisms underlying their membrane-molding activity and regulation. We end by highlighting the functional properties of select F-BAR domains that were elucidated by electron cryo-microscopy and 3D reconstruction of these modules while bound to flat and curved membranes.
| Original language | English (US) |
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| Journal | Madame Curie Bioscience Database |
| State | Published - 2008 |