Pombe Cdc15 homology proteins: regulators of membrane dynamics and the actin cytoskeleton

F-BAR domains: multifunctional regulators of membrane curvature

“…FasL is a member of the family of tumour-necrosisfactor-like ligands, induces apoptosis and has a role in the inflammatory response (Chitu and Stanley, 2007;Aspenstrom et al, 2006). The SH3 domain of PSTPIP1 can interact with a polyproline region of FasL, sequestering it in the secretory lysosomes of cytotoxic T cells and natural killer cells.…”

“…F-BAR proteins can generally be divided into six subfamilies: FES/FER tyrosine kinases, the PACSIN/syndapin subfamily, the CIP4 subfamily, the SRGAP subfamily, the PSTPIP subfamily and the FCHdomain-only (FCHO) subfamily (Aspenstrom et al, 2006;Chitu and Stanley, 2007). Primary sequence homology between the family members is low (Lippincott and Li, 2000), and similarity is defined mainly by the predicted domain structure.…”

F-BAR Proteins of the Syndapin Family Shape the Plasma Membrane and Are Crucial for Neuromorphogenesis

“…Syndapin I (also called PACSIN1) belongs to the F-BAR family within the BAR domain superfamily (Itoh et al, 2005)-a large and diverse protein family that can discern the curvature of a membrane by offering curved, crescent-shaped membrane interaction surfaces (Peter et al, 2004). Members of the F-BAR family are marked by the presence of a Fes/Cip4-homology (FCH) domain (Aspenström et al, 2006;Dawson et al, 2006;Chitu and Stanley, 2007). For syndapin I, the FCH domain has been shown to represent a self-association interface within a larger module, the extended F-BAR domain (eF-BAR), which is responsible for self-association in vivo (Kessels and Qualmann, 2006).…”

Phosphatidylinositol 4,5-Bisphosphate (PtdIns(4,5)P2) Specifically Induces Membrane Penetration and Deformation by Bin/Amphiphysin/Rvs (BAR) Domains

“…F-BAR or EFC domains (9,13) were identified from a group of proteins known as Pombe Cds15 homology proteins (25,26) that are involved in various actin-related processes, including clathrin-mediated endocytosis. F-BAR domains, like N-BAR domains, bind anionic lipids and induce vesicle tubulation in vitro (16,27) and cause tubulation of plasma membrane when overexpressed in mammalian cells (16,27,28).…”