The BAR domain proteins : Molding membranes in fission, fusion, and phagy
Identifieur interne : 009B77 ( Main/Exploration ); précédent : 009B76; suivant : 009B78The BAR domain proteins : Molding membranes in fission, fusion, and phagy
Auteurs : GANG REN [Australie, France] ; Parimala Vajjhala [Australie] ; Janet S. Lee [Australie] ; Barbara Winsor [France] ; Alan L. Munn [Australie]Source :
- Microbiology and molecular biology reviews [ 1092-2172 ] ; 2006.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
The Binl/amphiphysin/Rvsl67 (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 α-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.
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Munn</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Institute for Molecular Bioscience, University of Queensland</s1><s2>St. Lucia, Queensland 4072</s2><s3>AUS</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Australie</country><wicri:noRegion>St. Lucia, Queensland 4072</wicri:noRegion></affiliation><affiliation wicri:level="1"><inist:fA14 i1="03"><s1>ARC Special Research Centre for Functional and Applied Genomics, University of Queensland</s1><s2>St. Lucia, Queensland 4072</s2><s3>AUS</s3><sZ>5 aut.</sZ></inist:fA14><country>Australie</country><wicri:noRegion>St. Lucia, Queensland 4072</wicri:noRegion></affiliation><affiliation wicri:level="1"><inist:fA14 i1="04"><s1>School of Biomedical Sciences, University of Queensland</s1><s2>St. Lucia, Queensland 4072</s2><s3>AUS</s3><sZ>5 aut.</sZ></inist:fA14><country>Australie</country><wicri:noRegion>St. Lucia, Queensland 4072</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Microbiology and molecular biology reviews</title><title level="j" type="abbreviated">Microbiol. mol. biol. rev.</title><idno type="ISSN">1092-2172</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Microbiology and molecular biology reviews</title><title level="j" type="abbreviated">Microbiol. mol. biol. rev.</title><idno type="ISSN">1092-2172</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Fusion protein</term><term>Membrane protein</term><term>Review</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Protéine membranaire</term><term>Protéine fusion</term><term>Article synthèse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Binl/amphiphysin/Rvsl67 (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 α-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.</div></front></TEI><affiliations><list><country><li>Australie</li><li>France</li></country><region><li>Alsace (région administrative)</li><li>Grand Est</li></region><settlement><li>Strasbourg</li></settlement><orgName><li>Université Strasbourg 1</li></orgName></list><tree><country name="Australie"><noRegion><name sortKey="Gang Ren" sort="Gang Ren" uniqKey="Gang Ren" last="Gang Ren">GANG REN</name></noRegion><name sortKey="Lee, Janet S" sort="Lee, Janet S" uniqKey="Lee J" first="Janet S." last="Lee">Janet S. Lee</name><name sortKey="Munn, Alan L" sort="Munn, Alan L" uniqKey="Munn A" first="Alan L." last="Munn">Alan L. Munn</name><name sortKey="Munn, Alan L" sort="Munn, Alan L" uniqKey="Munn A" first="Alan L." last="Munn">Alan L. Munn</name><name sortKey="Munn, Alan L" sort="Munn, Alan L" uniqKey="Munn A" first="Alan L." last="Munn">Alan L. Munn</name><name sortKey="Vajjhala, Parimala" sort="Vajjhala, Parimala" uniqKey="Vajjhala P" first="Parimala" last="Vajjhala">Parimala Vajjhala</name></country><country name="France"><region name="Grand Est"><name sortKey="Gang Ren" sort="Gang Ren" uniqKey="Gang Ren" last="Gang Ren">GANG REN</name></region><name sortKey="Winsor, Barbara" sort="Winsor, Barbara" uniqKey="Winsor B" first="Barbara" last="Winsor">Barbara Winsor</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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