Elucidating molecular mechanism of mitochondrial membrane fusion in mitochondria using OPA1 proteoliposome
| Project/Area Number |
26840026
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Kurume University |
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Principal Investigator |
Tadato Ban 久留米大学, 分子生命科学研究所, 講師 (00579667)
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| Research Collaborator |
Ishihara Naotada 久留米大学, 分子生命科学研究所, 教授 (10325516)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | ミトコンドリア / 膜融合 / GTPase / プロテオリポソーム / カルジオリピン / リポソーム / OPA1 / 膜蛋白質 |
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| Outline of Final Research Achievements |
Mitochondria are highly dynamic organelles that undergo frequent fusion and fission. OPA1 is an essential GTPase protein for both mitochondrial inner membrane fusion and cristae structure. OPA1 is proteolytically processed into inner membrane-bound long isoforms (L-OPA1) and soluble short isoforms (S-OPA1). However, little is understood about how OPA1 regulate the membrane morphology. We have developed methods to express and purify human OPA1 using the BmNPV bacmid-silkworm expression system, and found that L-OPA1 on one side of membrane, and CL on the other side are sufficient for the fusion. GTP-independent heterotypic membrane tethering through L-OPA1 and CL primes the subsequent GTP-hydrolysis-dependent fusion, which can be modulated by the presence of S-OPA1. These results unveil the unique intracellular membrane fusion machinery unlike other fusogenic proteins, such as large GTPases mitofusins on mitochondrial outer membrane, and atlastins on endoplasmic reticulum
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Report
(4 results)
Research Products
(13 results)
