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dc.contributor.authorTakatsu, Hiroyuki-
dc.contributor.authorTakayama, Masahiro-
dc.contributor.authorNaito, Tomoki-
dc.contributor.authorTakada, Naoto-
dc.contributor.authorTsumagari, Kazuya-
dc.contributor.authorIshihama, Yasushi-
dc.contributor.authorNakayama, Kazuhisa-
dc.contributor.authorShin, Hye-Won-
dc.contributor.alternative申, 惠媛-
dc.description細胞膜の脂質輸送、セロトニンやヒスタミンの受容体で仕組みの一端を解明. 京都大学プレスリリース. 2017-11-17.-
dc.description.abstractWe and others showed that ATP11A and ATP11C, members of the P4-ATPase family, translocate phosphatidylserine (PS) and phosphatidylethanolamine from the exoplasmic to the cytoplasmic leaflets at the plasma membrane. PS exposure on the outer leaflet of the plasma membrane in activated platelets, erythrocytes, and apoptotic cells was proposed to require the inhibition of PS-flippases, as well as activation of scramblases. Although ATP11A and ATP11C are cleaved by caspases in apoptotic cells, it remains unclear how PS-flippase activity is regulated in non-apoptotic cells. Here we report that the PS-flippase ATP11C, but not ATP11A, is sequestered from the plasma membrane via clathrin-mediated endocytosis upon Ca2+-mediated PKC activation. Importantly, we show that a characteristic di-leucine motif (SVRPLL) in the C-terminal cytoplasmic region of ATP11C becomes functional upon PKC activation. Moreover endocytosis of ATP11C is induced by Ca2+-signaling via Gq-coupled receptors. Our data provide the first evidence for signal-dependent regulation of mammalian P4-ATPase.-
dc.publisherSpringer Nature-
dc.rights© The Author(s) 2017. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit
dc.subjectCalcium signalling-
dc.titlePhospholipid flippase ATP11C is endocytosed and downregulated following Ca2+-mediated protein kinase C activation-
dc.type.niitypeJournal Article-
dc.identifier.jtitleNature Communications-
dc.identifier.kakenJP15H01320 / JP16H00764 / JP17H03655-
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