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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy</title><author><name sortKey="Ren, Gang" sort="Ren, Gang" uniqKey="Ren G" first="Gang" last="Ren">Gang Ren</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Vajjhala, Parimala" sort="Vajjhala, Parimala" uniqKey="Vajjhala P" first="Parimala" last="Vajjhala">Parimala Vajjhala</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Lee, Janet S" sort="Lee, Janet S" uniqKey="Lee J" first="Janet S." last="Lee">Janet S. Lee</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Winsor, Barbara" sort="Winsor, Barbara" uniqKey="Winsor B" first="Barbara" last="Winsor">Barbara Winsor</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Munn, Alan L" sort="Munn, Alan L" uniqKey="Munn A" first="Alan L." last="Munn">Alan L. Munn</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16524918</idno><idno type="pmc">1393252</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1393252</idno><idno type="RBID">PMC:1393252</idno><idno type="doi">10.1128/MMBR.70.1.37-120.2006</idno><date when="2006">2006</date><idno type="wicri:Area/Pmc/Corpus">001028</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001028</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy</title><author><name sortKey="Ren, Gang" sort="Ren, Gang" uniqKey="Ren G" first="Gang" last="Ren">Gang Ren</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Vajjhala, Parimala" sort="Vajjhala, Parimala" uniqKey="Vajjhala P" first="Parimala" last="Vajjhala">Parimala Vajjhala</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Lee, Janet S" sort="Lee, Janet S" uniqKey="Lee J" first="Janet S." last="Lee">Janet S. Lee</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Winsor, Barbara" sort="Winsor, Barbara" uniqKey="Winsor B" first="Barbara" last="Winsor">Barbara Winsor</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Munn, Alan L" sort="Munn, Alan L" uniqKey="Munn A" first="Alan L." last="Munn">Alan L. Munn</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">Microbiology and Molecular Biology Reviews</title><idno type="ISSN">1092-2172</idno><idno type="eISSN">1098-5557</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>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 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.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Microbiol Mol Biol Rev</journal-id><journal-id journal-id-type="publisher-id">mmbr</journal-id><journal-title>Microbiology and Molecular Biology Reviews</journal-title><issn pub-type="ppub">1092-2172</issn><issn pub-type="epub">1098-5557</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">16524918</article-id><article-id pub-id-type="pmc">1393252</article-id><article-id pub-id-type="publisher-id">0029-05</article-id><article-id pub-id-type="doi">10.1128/MMBR.70.1.37-120.2006</article-id><article-categories><subj-group subj-group-type="heading"><subject>Reviews</subject></subj-group></article-categories><title-group><article-title>The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Ren</surname><given-names>Gang</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">4</xref></contrib><contrib contrib-type="author"><name><surname>Vajjhala</surname><given-names>Parimala</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Lee</surname><given-names>Janet S.</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Winsor</surname><given-names>Barbara</given-names></name><xref ref-type="aff" rid="aff1">4</xref></contrib><contrib contrib-type="author"><name><surname>Munn</surname><given-names>Alan L.</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="aff" rid="aff1">2</xref><xref ref-type="aff" rid="aff1">3</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="aff1">Institute for Molecular Bioscience,<label>1</label> ARC Special Research Centre for Functional and Applied Genomics,<label>2</label> School of Biomedical Sciences, University of Queensland, St. Lucia, Queensland 4072, Australia,<label>3</label> UMR7156, Centre National Recherche Scientifique, Université Louis Pasteur, Strasbourg 67084, France<label>4</label></aff><author-notes><fn id="cor1"><label>*</label><p>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: <email>a.munn@imb.uq.edu.au</email>.</p></fn></author-notes><pub-date pub-type="ppub"><month>3</month><year>2006</year></pub-date><volume>70</volume><issue>1</issue><fpage>37</fpage><lpage>120</lpage><copyright-statement>Copyright © 2006, American Society for Microbiology</copyright-statement><copyright-year>2006</copyright-year><abstract><p>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 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.</p></abstract><custom-meta-wrap><custom-meta><meta-name>PDF filename</meta-name><meta-value>zmr00106000037</meta-value></custom-meta></custom-meta-wrap></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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