2013 Fiscal Year Final Research Report
Molecular mechanism for regulaiton of ion transporter via lipid signaling and its structural basis
| Project/Area Number |
23390046
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General physiology
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| Research Institution | National Cardiovascular Center Research Institute |
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Principal Investigator |
WAKABAYASHI Shigeo 独立行政法人国立循環器病研究センター, 研究所, 部長 (70158583)
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| Co-Investigator(Renkei-kenkyūsha) |
TAKEDA Souichi 独立行政法人国立循環器病研究センター研究所, 室長 (80332279)
IWATA Yuko 独立行政法人国立循環器病研究センター研究所, 室長 (80171908)
NISHITANI Tomoe 独立行政法人国立循環器病研究センター研究所, 室長 (50393244)
HISAMITSU Takashi 独立行政法人国立循環器病研究センター研究所, 室長 (50327946)
KOBAYASHI Soushi 独立行政法人国立循環器病研究センター研究所, 研究員 (50511531)
SHIMADA Naoko 独立行政法人国立循環器病研究センター研究所, 流動研究員 (60600385)
KAMAUCHI Shinya 独立行政法人国立循環器病研究センター研究所, 流動研究員 (00397564)
NAKAO Shu 独立行政法人国立循環器病研究センター研究所, 流動研究員 (30646956)
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| Project Period (FY) |
2011-04-01 – 2014-03-31
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| Keywords | トランスポータ / 生理活性脂質 / 結晶構造 / 創薬 / 細胞内イオン制御 |
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| Research Abstract |
Although plasma membrane ion transports are delicately controlled by many signals, its breakdown contributes to exacerbation of various diseases. In this research, we studied in details about the regulatory mechanism of mammalian Na+/H+ exchanger NHE1, which was unknown until now. We found that NHE1 is an ATP binding protein, and that NHE1 activity is maintained by direct binding of ATP. Furthermore, hormonal activation of NHE1 was found to occur by the switching mechanism between ATP and bioactive lipids (diacylglycerol, etc.) via lipid-interacting domain of NHE1. Moreover, activation of NHE1 was found to amplify the NFAT signaling via calcineurin which directly interacts with NHE1.
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[Journal Article] Perilipin 5, a lipid droplet-binding protein, protects heart from oxidative burden by sequestering fatty acid from excessive oxidation2012
Author(s)
Kuramoto K, Okamura T, Yamaguchi T, Nakamura TY, Wakabayashi S, Morinaga H, Nomura M, Yanase T, Otsu K, Usuda N, Matsumura S, Inoue K, Fushiki T, Kojima Y, Hashimoto T, Sakai F, Hirose F, Osumi T
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Journal Title
J Biol. Chem
Volume: 287(28)
Pages: 23852-23863
DOI
Peer Reviewed
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