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QuickView for F-BAR domain (biogroup)
- Description:
- All eukaryotic cells are surrounded by a plasma membrane, and they alsocontain multiple membrane-based organelles and structures inside cells. Thusmembrane remodeling is likely to be important for most cellular activities anddevelopment. The Bin-Amphiphysin-Rvs (BAR) domain superfamily of proteins hasbeen found to play a major role in remodeling cellular membranes linked withorganelle biogenesis, membrane trafficking, cell division, cell morphology andcell migration. The BAR domain superfamily of proteins is evolutionarilyconserved with representative members present from yeast to man. Currentlythere are three distinct families of BAR domain proteins: classical BAR, F-BAR (FCH-BAR e.g., Fes/CIP4 homology BAR e.g., Toca-1) and I-BAR (inverse-BAR e.g., IRSp53). The classical BAR, F-BAR, and I-BAR domainsare structurally similar homodimeric modules with antiparallel arrangement ofmonomers.The F-BAR domain is emerging as an important player in membrane remodelingpathways. F-BAR domain proteins couple membrane remodeling with actin dynamicsassociated with endocytic pathways and filopodium formation. F-BAR domaincontaining proteins can be categorized into five sub-families based on theirphylogeny which is consistent with the additional protein domains theypossess, for example, RhoGAP domains, Cdc42 binding sites,SH2 domains, SH3 domains and tyrosinekinase domains.The N-terminal part (about one third) of the F-BAR domain was previouslycharacterised as an FCH (FER-CIP4 homology) domain. However, the region ofsequence similarity extends to an adjacent region with a coiled-coil (CC)structure. Hence, the F-BAR domain (FCH+CC, ~300 amino acids) has also beencalled extended FC (EFC) domain. The F-BAR domain plays a role in dimerizationand membrane phospholipid binding. It binds specifically to certain kinds oflipids and acts as a a dimeric membrane-binding curvature effector.The F-BAR domain is composed of five helices. Its structure is composed of ashort N-terminal helix, three long alpha helices, and a short C-terminal helixfollowed by an extended peptide of 17 amino acids.
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