The BAR domain proteins: Molding membranes in fission, fusion, and phagy

Ren, G., Vajjhala, P., Lee, J. S., Winsor, B. and Munn, A. L. (2006) The BAR domain proteins: Molding membranes in fission, fusion, and phagy. Microbiology And Molecular Biology Reviews, 70 1: 37-120. doi:10.1128/MMBR.70.1.37-120.2006

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Author Ren, G.
Vajjhala, P.
Lee, J. S.
Winsor, B.
Munn, A. L.
Title The BAR domain proteins: Molding membranes in fission, fusion, and phagy
Journal name Microbiology And Molecular Biology Reviews   Check publisher's open access policy
ISSN 1092-2172
Publication date 2006-03
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1128/MMBR.70.1.37-120.2006
Open Access Status File (Publisher version)
Volume 70
Issue 1
Start page 37
End page 120
Total pages 84
Editor Diana Downs
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2006
Language eng
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.
Keyword Microbiology
Synaptic Vesicle Endocytosis
Clathrin-mediated Endocytosis
Cyclin-dependent Kinase-5
Yeast Saccharomyces-cerevisiae
Aldrich-syndrome Protein
Dynamin-related Gtpase
Cortical Actin Cytoskeleton
Growth-hormone Receptor
Stiff-man Syndrome
Cultured Hippocampal-neurons
Q-Index Code C1

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Excellence in Research Australia (ERA) - Collection
2007 Higher Education Research Data Collection
School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 120 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 123 times in Scopus Article | Citations
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Created: Wed, 15 Aug 2007, 09:06:23 EST