Downloads: 1581

Files in This Item:
File Description SizeFormat 
Suzuki_et_al.pdf6.34 MBAdobe PDFView/Open
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSuzuki, Junen
dc.contributor.authorUmeda, Masatoen
dc.contributor.authorSims, Peter Jen
dc.contributor.authorNagata, Shigekazuen
dc.contributor.alternative鈴木, 淳ja
dc.contributor.alternative梅田, 眞郷ja
dc.contributor.alternative長田, 重一ja
dc.date.accessioned2010-11-29T01:05:29Z-
dc.date.available2010-11-29T01:05:29Z-
dc.date.issued2010-11-24-
dc.identifier.issn0028-0836-
dc.identifier.urihttp://hdl.handle.net/2433/131831-
dc.description血小板において止血の引き金となるリン脂質の暴露に関与する因子の同定-ヒトの遺伝病(スコット症候群)の原因遺伝子の同定. 京都大学プレスリリース. 2010-11-25.ja
dc.description.abstractIn all animal cells, phospholipids are asymmetrically distributed between the outer and inner leaflets of the plasma membrane. This asymmetrical phospholipid distribution is disrupted in various biological systems. For example, when blood platelets are activated, they expose phosphatidylserine (PtdSer) to trigger the clotting system. The PtdSer exposure is believed to be mediated by Ca(2+)-dependent phospholipid scramblases that transport phospholipids bidirectionally, but its molecular mechanism is still unknown. Here we show that TMEM16F (transmembrane protein 16F) is an essential component for the Ca(2+)-dependent exposure of PtdSer on the cell surface. When a mouse B-cell line, Ba/F3, was treated with a Ca(2+) ionophore under low-Ca(2+) conditions, it reversibly exposed PtdSer. Using this property, we established a Ba/F3 subline that strongly exposed PtdSer by repetitive fluorescence-activated cell sorting. A complementary DNA library was constructed from the subline, and a cDNA that caused Ba/F3 to expose PtdSer spontaneously was identified by expression cloning. The cDNA encoded a constitutively active mutant of TMEM16F, a protein with eight transmembrane segments. Wild-type TMEM16F was localized on the plasma membrane and conferred Ca(2+)-dependent scrambling of phospholipids. A patient with Scott syndrome, which results from a defect in phospholipid scrambling activity, was found to carry a mutation at a splice-acceptor site of the gene encoding TMEM16F, causing the premature termination of the protein.en
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherNature Publishing Groupen
dc.rights許諾条件により本文は2011-05-24に公開.ja
dc.rightsこの論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。ja
dc.rightsThis is not the published version. Please cite only the published version.en
dc.titleCalcium-dependent phospholipid scrambling by TMEM16F.en
dc.typejournal article-
dc.type.niitypeJournal Article-
dc.identifier.ncidAA00752384-
dc.identifier.jtitleNatureen
dc.identifier.volume468-
dc.identifier.issue7325-
dc.identifier.spage834-
dc.identifier.epage838-
dc.relation.doi10.1038/nature09583-
dc.textversionauthor-
dc.startdate.bitstreamsavailable2011-05-24-
dc.identifier.pmid21107324-
dc.relation.urlhttps://www.kyoto-u.ac.jp/static/ja/news_data/h/h1/news6/2010/101125_1.htm-
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.