Structural and functional analyses of VAT-1, a phospholipid transfer protein between the ER and mitochondria
| Project/Area Number |
16K21473
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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
Cell biology
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| Research Institution | Ehime University (2017)
Kyoto Sangyo University (2016) |
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Principal Investigator |
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | リン脂質輸送タンパク質 / 結晶構造解析 / オルガネラ間リン脂質輸送 / ミトコンドリア / 小胞体 / リン脂質 |
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| Outline of Final Research Achievements |
Phospholipid trafficking between organelles is necessary for the achievement of membrane-specific phospholipid compositions. Here we focused on VAT1, which involves phosphatidylserine (PS) transfer from the endoplasmic reticulum (ER) to mitochondria, and determined the crystal structure of VAT1. Crystal structure of VAT1 and structure-based mutational analyses indicates acidic phospholipid binding region and an exposed flexible loop region which is important for the acidic phospholipid transfer and acidic membrane binding. We also showed that basic residues and two tryptophan residues in the exposed flexible loop region are important for acidic phospholipid transfer and acidic membrane binding and that these tryptophan residues are buried into the acidic membranes upon binding. These results provide the structural basis for understanding the molecular mechanism of phospholipid transfer between the ER and mitochondria.
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Report
(3 results)
Research Products
(4 results)
