Abstract
The F-BAR-domain-containing proteins (F-BAR proteins) are a group of adaptor proteins, members of which are found in all eukaryotes except plants. Also known as Pombe/Cdc15 homology (PCH)-family proteins, they have essential roles in fundamental biological processes, such as endocytosis, exocytosis
Highlights
Amphiphysin/RVS (BAR) domains (Itoh et al, 2005; Tsujita et al, 2006)
The most striking evidence for the involvement of F-BAR proteins in endocytosis came from the observation by Kamioka and colleagues (Kamioka et al, 2004), who reported that FBP17 induces tubular invaginations of the plasma membrane, and that the F-BAR domain is necessary and sufficient for this
A mutant form of FBP17 that is unable to bind to dynamin induces the formation of tubules that remain attached to the plasma membrane, leading the authors to conclude that the FBAR domain acts in a manner similar to BAR domains and that an interaction with dynamin is required for endocytosis
Summary
Homology between the family members is low (Lippincott and Li, 2000), and similarity is defined mainly by the predicted domain structure. The crystal structures of the N-BAR and BAR domains have revealed that they are crescent-shaped dimers binding to highly curved membranes (outer radius ~11-15 nm) via the concave surface of the protein (Gallop and McMahon, 2005). The recent determination of the crystal structures of the F-BAR domains of mammalian FCHO2, FBP17 and CIP4 reveals that these domains are structurally similar to BAR domains – characteristically, an elongated dimer formed by the antiparallel interaction of two α-helical coiled coils, each a three-helical bundle (Henne et al, 2007; Shimada et al, 2007) This consolidates a trend among membranebending proteins that contain BAR, NBAR or F-BAR domains: the consequence of domain dimerization is the formation of a central six-helical bundle, from which two helices protrude on either side. The mechanistic connections between F-BAR proteins and huntingtin are unclear
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