The state of F-BAR domains as membrane-bound oligomeric platforms

Fes/Cip4 homology Bin/amphiphysin/Rvs (F-BAR) domains, like all BAR domains, are dimeric units that oligomerize and bind membranes. F-BAR domains are generally coupled to additional domains that function in protein binding or have enzymatic activity. Because of their crescent shape and ability to oligomerize, F-BAR domains have been traditionally viewed as membrane-deformation modules. However, multiple independent studies have provided no evidence that certain F-BAR domains are able to tubulate membrane. Instead, a growing body of literature featuring structural, biochemical, biophysical, and microscopy-based studies supports the idea that the F-BAR domain family can be unified only by their ability to form oligomeric assemblies on membranes to provide platforms for molecular assembly. Fes/Cip4 homology Bin/amphiphysin/Rvs (F-BAR) domains are membrane-binding modules that oligomerize and couple actin-based structures to membranes.Although most F-BAR domains are observed to tubulate membranes in vitro, a subset of F-BAR domains lacking membrane tubulation activity have been identified, suggesting that membrane-tubulation activity does not unify F-BAR family function.F-BAR domains employ diverse schemes of oligomerization and the oligomerization mode of a particular F-BAR domain dictates whether it can generate membrane curvature.F-BAR domain oligomers polymerize protein interaction networks on membranes in part through the recruitment of direct F-BAR domain-binding proteins. Disruption of these membrane-proximal interactions can impact the organization of an entire actin-based structure.Modes of F-BAR domain oligomerization and binding partners are specialized depending on cellular context.