2013 Fiscal Year Final Research Report
Regulation of glycosphingolipids biosynthesis by multi-spanning transmembrane protein family TMBIMs and their molecular machinery
| Project/Area Number |
23770164
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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 |
Functional biochemistry
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| Research Institution | National Institute of Infectious Diseases |
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Principal Investigator |
YAMAJI Toshiyuki 国立感染症研究所, 細胞化学部, 主任研究官 (50332309)
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| Project Period (FY) |
2011 – 2013
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| Keywords | スフィンゴ糖脂質 / TMBIMファミリー / FAIM2 |
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| Research Abstract |
In this study, I examined new functions of FAIM2, a member of TMBIM family, based on my previous report that TMBIM family members reduced a glycosphingolipid, Gb3. Consequently, I found the following points: (1) FAIM2 interacted with NEDD4 E3 ligase family proteins through the N-terminal cytosolic domain of FAIM2; (2) an aspartate residue that is commonly observed in the multi-spanning membrane domains of TMBIM family was critical for two activities of FAIM2, the inhibitory activity to FAS-mediated apoptosis and Gb3-reducing activity. On the other hand, as a new tool to analyze glycolipid metabolism, I established a series of HeLa cell mutants deficient in sphingolipid-related genes including glucosylceramide synthase using TALENs.
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Author(s)
Kukimoto I, Maehama T, Sekizuka T, Ogasawara Y, Kondo K, Kusumoto-Matsuo R, Mori S, Ishii Y, Takeuchi T, Yamaji T, Takeuchi F, Hanada K, Kuroda M.
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Journal Title
PLoS One
Volume: 8
Pages: e80583
Peer Reviewed
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Miyazaki K, Sakuma K, Kawamura YI, Izawa M, Ohmori K, Mitsuki M, Yamaji T, Hashimoto Y, Suzuki A, Saito Y, Dohi T, Kannagi R.
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Journal Title
J Immunol
Volume: 188
Pages: 4690-700
Peer Reviewed
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