| Project/Area Number |
25293049
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
General physiology
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| Research Institution | Keio University |
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Principal Investigator |
SOHMA Yoshiro 慶應義塾大学, 医学部, 准教授 (60268183)
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| Co-Investigator(Renkei-kenkyūsha) |
UCHIHASHI Takayuki 金沢大学, 数物科学系, 准教授 (30326300)
NISHIZAKA Takayuki 学習院大学, 理学部, 教授 (40359112)
SAKURAI Minoru 東京工業大学, バイオ研究基盤支援総合センター, 教授 (50162342)
SATO Chikara 独立行政法人産業技術総合研究所, バイオメディカル研究部門, 研究グループ長 (00357146)
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| Research Collaborator |
YAMASHITA Hayato
YU Ying-Chun
HWANG Tzyh-Chang
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| Project Period (FY) |
2013-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥17,030,000 (Direct Cost: ¥13,100,000、Indirect Cost: ¥3,930,000)
Fiscal Year 2015: ¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2014: ¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2013: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
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| Keywords | ABCトランスポ－タ－ / ATP加水分解 / NBDドメイン / 膜輸送 / 分子間相互作用 / 抗原－抗体反応 / 原子間力顕微鏡 / 抗原抗体反応 / ABCトランスポーター |
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| Outline of Final Research Achievements |
ABC transporter superfamily is one of the biggest protein families which members play essential physiological roles in human. The members in the ABC transporter superfamily share highly-conserved Nucleotide Binding Domain (NBD) underlying their ATP-driven mechanisms. We investigated molecular mechanism of the ‘NBD engine’ in an ABC member, Cystic Fibrosis Transmembrane Regulator (CFTR) using single-molecular measuring methods including high-speed atomic force microscopy (HS-AFM).
We succeeded the first direct observation of dynamics of the intracellular complex consisting of two NBDs and regulatory (R) domain in CFTR using HS-AFM. We also obtained results in the direct observations of binding/unbinding process between AQP4 and anti-AQP4 antibody as a model of the molecule-molecule interactions. In addition, we performed several molecular physiological/pharmacological studies for disease-associated CFTR mutants.
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