{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670321173210752.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1093/jb/mvq049"}},{"identifier":{"@type":"URI","@value":"http://academic.oup.com/jb/article-pdf/148/1/1/2636303/mvq049.pdf"}},{"identifier":{"@type":"PMID","@value":"20435640"}}],"dc:title":[{"@value":"The proposed functions of membrane curvatures mediated by the BAR domain superfamily proteins"}],"description":[{"notation":[{"@value":"The plasma membrane, the outermost surface of eukaryotic cells, contains various substructures, such as protrusions or invaginations, which are associated with diverse functions, including endocytosis and cell migration. These structures of the plasma membrane can be considered as tubules or inverted tubules (protrusions) of the membrane. There are six modes of membrane curvature at the plasma membrane, which are classified by the positive or negative curvature and the location of the curvature (tip, neck or shaft of the tubules). The BAR domain superfamily proteins have structurally determined positive and negative curvatures of membrane contact at their BAR, F-BAR and I-BAR domains, which generate and maintain such curved membranes by binding to the membrane. Importantly, the SH3 domains of the BAR domain superfamily proteins bind to the actin regulatory WASP/WAVE proteins, and the BAR/F-BAR/I-BAR domain-SH3 unit could orient the actin filaments towards the membrane for each subcellular structure. These membrane tubulations are also considered to function in membrane fusion and fission."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380004233478819469","@type":"Researcher","foaf:name":[{"@value":"S. Suetsugu"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"0021924X"}],"prism:publicationName":[{"@value":"Journal of Biochemistry"}],"dc:publisher":[{"@value":"Oxford University Press (OUP)"}],"prism:publicationDate":"2010-04-30","prism:volume":"148","prism:number":"1","prism:startingPage":"1","prism:endingPage":"12"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","url":[{"@id":"http://academic.oup.com/jb/article-pdf/148/1/1/2636303/mvq049.pdf"}],"createdAt":"2010-05-01","modifiedAt":"2020-06-04","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Actin%20Cytoskeleton","dc:title":"Actin Cytoskeleton"},{"@id":"https://cir.nii.ac.jp/all?q=Multigene%20Family","dc:title":"Multigene Family"},{"@id":"https://cir.nii.ac.jp/all?q=Cell%20Membrane","dc:title":"Cell Membrane"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Humans","dc:title":"Humans"},{"@id":"https://cir.nii.ac.jp/all?q=Membrane%20Proteins","dc:title":"Membrane Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Disease","dc:title":"Disease"},{"@id":"https://cir.nii.ac.jp/all?q=Cell%20Surface%20Extensions","dc:title":"Cell Surface Extensions"},{"@id":"https://cir.nii.ac.jp/all?q=Membrane%20Fusion","dc:title":"Membrane Fusion"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Structure,%20Tertiary","dc:title":"Protein Structure, Tertiary"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050858784329458560","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Filopodium-derived vesicles produced by MIM enhance the migration of recipient cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1360002216925049344","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Membrane re-modelling by BAR domain superfamily proteins via molecular and non-molecular factors"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004233478819200","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Salt Bridge Formation between the I-BAR Domain and Lipids Increases Lipid Density and Membrane Curvature"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285708954251392","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"The F-BAR Protein Rapostlin Regulates Dendritic Spine Formation in Hippocampal Neurons"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285711312576384","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Dynamic Shaping of Cellular Membranes by Phospholipids and Membrane-Deforming Proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092525313664","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Physical Properties and Reactivity of Microdomains in Phosphatidylinositol-Containing Supported Lipid Bilayer"}]},{"@id":"https://cir.nii.ac.jp/crid/1360576118715604736","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"PMP2/FABP8 induces PI(4,5)P2-dependent transbilayer reorganization of sphingomyelin in the plasma membrane"}]},{"@id":"https://cir.nii.ac.jp/crid/1360846641606434048","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Physicochemical Analysis from Real-Time Imaging of Liposome Tubulation Reveals the Characteristics of Individual F-BAR Domain Proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848657077241472","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Effect of amino acid distribution of amphipathic helical peptide derived from human apolipoprotein A‐I on membrane curvature sensing"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1093/jb/mvq049"},{"@type":"OPENAIRE","@value":"doi_dedup___::044e72cb90f82386a454dd7b11d0588b"},{"@type":"CROSSREF","@value":"10.1042/bst20170322_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.1038/s41598-017-06334-5_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.1016/j.devcel.2021.02.029_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.1074/jbc.m111.236265_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.1152/physrev.00040.2013_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.3390/membranes11050339_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.1016/j.celrep.2021.109935_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.1016/j.febslet.2013.01.026_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"},{"@type":"CROSSREF","@value":"10.1021/la303902q_references_DOI_RUFhe2nqE6LrY67E3JM3wSMzmm6"}]}