Molecular basis of P-type ion pumps and diseases caused by pump defects.
| Project/Area Number |
23370058
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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 |
Functional biochemistry
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| Research Institution | Asahikawa Medical College |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
YAMASAKI Kazuo 旭川医科大学, 医学部, 講師 (60241428)
DAIHO Takashi 旭川医科大学, 医学部, 准教授 (90207267)
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| Project Period (FY) |
2011-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥19,890,000 (Direct Cost: ¥15,300,000、Indirect Cost: ¥4,590,000)
Fiscal Year 2014: ¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2013: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2012: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2011: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
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| Keywords | P型カチオン輸送ATPase / Ca-ATPase / リン酸化反応中間体 / 反応中間体構造アナログ / 筋小胞体 / 能動輸送 / エネルギー共役 / 反応機構 / Caポンプ / リン酸化中間体 / 小胞体 / 部位特異的変異 / 構造変化 / カルシウムポンプ / 構造機能連関 / Ca-pump / Sarcoplasmic reticulum / Phosphorylation / Structural analog / Metal fluoride / Reaction intermediate / Active transport / Sarco(endo)plasmic reticulum / Phosphorylated intermediate |
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| Outline of Final Research Achievements |
P-type ATPases possess common domain-structure and couple the ATP hydrolysis with the specific cation-transport. In this study, we first revealed by extensive mutations and kinetic analyses of Ca-ATPase that the second transmembrane helix plays critical roles via its motions and changes in its secondary structure for transferring the motions of cytoplasmic domains to the transmembrane cation transport sites there by for the energy coupling. We also revealed that unique structural fluctuation is equipped in each of the phosphoenzyme intermediates, and the fluctuation functions to accomplish the proper forward transport reaction. Thus we contributed to the comprehensive understanding of the P-type ATPase mechanism and an establishment of molecular basis for diseases developed by the pump defects.
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Report
(5 results)
Research Products
(25 results)
