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dc.contributor.authorRen, Gang
dc.contributor.authorVajjhala, Parimala
dc.contributor.authorS. Lee, Janet
dc.contributor.authorWinsor, Barbara
dc.contributor.authorL. Munn, Alan
dc.contributor.editorDiana Downs
dc.date.accessioned2017-09-05T01:03:31Z
dc.date.available2017-09-05T01:03:31Z
dc.date.issued2006
dc.date.modified2009-12-07T07:55:05Z
dc.identifier.issn10922172
dc.identifier.doi10.1128/MMBR.70.1.37-120.2006
dc.identifier.urihttp://hdl.handle.net/10072/27203
dc.description.abstractThe 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 -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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoen_AU
dc.publisherAmerican Society for Microbiology
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom37
dc.relation.ispartofpageto120
dc.relation.ispartofissue1
dc.relation.ispartofjournalMicrobiology and Molecular Biology Reviews
dc.relation.ispartofvolume70
dc.rights.retentionY
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchTechnology
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode10
dc.subject.fieldofresearchcode11
dc.titleThe BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dc.description.versionPublished
gro.rights.copyright© 2006 American Society for Microbiology. The attached file is reproduced here in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
gro.date.issued2006
gro.hasfulltextFull Text
gro.griffith.authorMunn, Alan L.


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