Downloads: 281

Files in This Item:
File Description SizeFormat 
jcb.201607086.pdf3.56 MBAdobe PDFView/Open
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKinoshita, Masanaoen
dc.contributor.authorSuzuki, Kenichi G.N.en
dc.contributor.authorMatsumori, Nobuakien
dc.contributor.authorTakada, Misaen
dc.contributor.authorAno, Hikaruen
dc.contributor.authorMorigaki, Kenichien
dc.contributor.authorAbe, Mitsuhiroen
dc.contributor.authorMakino, Asamien
dc.contributor.authorKobayashi, Toshihideen
dc.contributor.authorHirosawa, Koichiro M.en
dc.contributor.authorFujiwara, Takahiro K.en
dc.contributor.authorKusumi, Akihiroen
dc.contributor.authorMurata, Michioen
dc.contributor.alternative木下, 祥尚ja
dc.contributor.alternative鈴木, 健一ja
dc.contributor.alternative松森, 信明ja
dc.contributor.alternative楠見, 明弘ja
dc.contributor.alternative村田, 道雄ja
dc.date.accessioned2017-03-28T02:29:33Z-
dc.date.available2017-03-28T02:29:33Z-
dc.date.issued2017-03-22-
dc.identifier.issn0021-9525-
dc.identifier.urihttp://hdl.handle.net/2433/219127-
dc.description脂質の挙動をありのままに再現する蛍光プローブでラフトの形成機構を解明. 京都大学プレスリリース. 2017-03-28.ja
dc.description.abstractSphingomyelin (SM) has been proposed to form cholesterol-dependent raft domains and sphingolipid domains in the plasma membrane (PM). How SM contributes to the formation and function of these domains remains unknown, primarily because of the scarcity of suitable fluorescent SM analogs. We developed new fluorescent SM analogs by conjugating a hydrophilic fluorophore to the SM choline headgroup without eliminating its positive charge, via a hydrophilic nonaethylene glycol linker. The new analogs behaved similarly to the native SM in terms of their partitioning behaviors in artificial liquid order-disorder phase-separated membranes and detergent-resistant PM preparations. Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone{textendash}dependent manners, and that, for ~{}10{textendash}50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size{textendash}, cholesterol-, and GPI anchoring{textendash}dependent manners. These results suggest that SM continually and rapidly exchanges between CD59-associated raft domains and the bulk PM.en
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherRockefeller University Pressen
dc.rights© 2017 Kinoshita et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http ://www .rupress .org /terms /). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https ://creativecommons .org /licenses /by -nc -sa /4 .0 /).en
dc.titleRaft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogsen
dc.typejournal article-
dc.type.niitypeJournal Article-
dc.identifier.jtitleThe Journal of Cell Biologyen
dc.identifier.volume216-
dc.identifier.issue4-
dc.identifier.spage1183-
dc.identifier.epage1204-
dc.relation.doi10.1083/jcb.201607086-
dc.textversionpublisher-
dc.identifier.pmid28330937-
dc.relation.urlhttps://www.kyoto-u.ac.jp/ja/research-news/2017-03-28-0-
dcterms.accessRightsopen access-
Appears in Collections:Journal Articles

Show simple item record

Export to RefWorks


Export Format: 


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.