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Microbiology and Molecular Biology Reviews, March 2006, p. 37-120, Vol. 70, No. 1
1092-2172/06/$08.00+0     doi:10.1128/MMBR.70.1.37-120.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Gang Ren,1,4 Parimala Vajjhala,1 Janet S. Lee,1 Barbara Winsor,4 and Alan L. Munn1,2,3*

Institute for Molecular Bioscience,1 ARC Special Research Centre for Functional and Applied Genomics,2 School of Biomedical Sciences, University of Queensland, St. Lucia, Queensland 4072, Australia,3 UMR7156, Centre National Recherche Scientifique, Université Louis Pasteur, Strasbourg 67084, France4

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.

* Corresponding author. Mailing address: Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia. Phone: 61-7-3346 2017. Fax: 61-7-3346 2101. E-mail: a.munn{at}imb.uq.edu.au.

Microbiology and Molecular Biology Reviews, March 2006, p. 37-120, Vol. 70, No. 1
1092-2172/06/$08.00+0     doi:10.1128/MMBR.70.1.37-120.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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