title: The BAR domain proteins: molding membranes in fission, fusion, and phagy.
abstract: The Bin1/amphiphysin/Rvs167 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt alpha-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.
authors.affiliation: Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
authors.forename: Gang
authors.initials: G
authors.lastname: Ren
authors.forename: Parimala
authors.initials: P
authors.lastname: Vajjhala
authors.forename: Janet S
authors.initials: JS
authors.lastname: Lee
authors.forename: Barbara
authors.initials: B
authors.lastname: Winsor
authors.forename: Alan L
authors.initials: AL
authors.lastname: Munn
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D004718:Saccharomycetales / Q000378:metabolism; D012568:Schizosaccharomyces / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D005656:Fungal Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C075637:amphiphysin