Abstract
Eukaryotic cells have complicated membrane systems. The outermost plasma membrane contains various substructures, such as invaginations and protrusions, which are involved in endocytosis and cell migration. Moreover, the intracellular membrane compartments, such as autophagosomes and endosomes, are essential for cellular viability. The Bin-Amphiphysin-Rvs167 (BAR) domain superfamily proteins are important players in membrane remodeling through their structurally determined membrane binding surfaces. A variety of BAR domain superfamily proteins exist, and each family member appears to be involved in the formation of certain subcellular structures or intracellular membrane compartments. Most of the BAR domain superfamily proteins contain SH3 domains, which bind to the membrane scission molecule, dynamin, as well as the actin regulatory WASP/WAVE proteins and several signal transduction molecules, providing possible links between the membrane and the cytoskeleton or other machineries. In this review, we summarize the current information about each BAR superfamily protein with an SH3 domain(s). The involvement of BAR domain superfamily proteins in various diseases is also discussed.
Highlights
The relationship between cellular morphology and diseases, such as cancer, has been unclear.transformed cancer cells are often first recognized by changes in their morphology
The N-BAR domain is included in the BAR subfamily that contains amino acids that form an amphipathic helix upon membrane binding in front of the BAR domain fold
By using knock-out mice of all three endophilin A isoforms, it was demonstrated that all three endophilins, A1, A2, and A3, are involved in the recycling of synaptic vesicles at the uncoating stage of clathrin-coated vesicles (CCVs), rather than the scission of CCPs
Summary
The relationship between cellular morphology and diseases, such as cancer, has been unclear. Dynamic remodeling of the membrane is achieved by the interplay between proteins and lipids Among these proteins, accumulating evidence indicates that the Bin-Amphiphysin-Rvs167 (BAR) domain superfamily proteins (referred to hereafter as BAR proteins) play key roles. The BAR domains typically form a dimer, which is the unit for membrane binding. Each dimer possesses a distinct curved surface, from almost flat like Pinkbar to those of various steepness, where the basic-charged amino acid residues form a cluster, and deforms the membrane through the binding of the curved surface to the negatively-charged phospholipids in the plasma membrane (Figure 2). Most of the SH3 domains bind to WASP family proteins and dynamin. The BAR domain superfamily proteins that are coupled to dynamin, WASP/WAVE family proteins, and other proteins are involved in several biological functions, including regulation of both the cytoskeleton and membrane shape. We describe some BAR proteins that lack the SH3 domain, which regulate the actin cytoskeleton
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