| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2018: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Outline of Final Research Achievements |
Wnt signaling pathway plays an important role in determination for cell fate, such as embryonic development. The cytoplasmic signaling proteins, Axin, Coiled-coil-DIX1 (Ccd1), and Dvl form the platform for cytoplasmic signal transduction by making the dynamic oligomer through the homotypic and heterotypic interaction. In this study, we determined the crystal structure of Axin-Ccd1 heteroligomer forming the DIX domains conserved at both proteins. The structure of Axin-Ccd1 heterooligomer revealed the detail of the heterotypic interaction between the DIX domains and the rearrangement of the Axin homooligomer induced by the Ccd1-binding. The fluorescence resonance energy transfer measurement and mutation study indicated that Ccd1 induces the rearrangement of Axin homooligmer in solution by the heterotypic interaction. These findings suggest the requirement investigating the relationship between the rearrangement of Axin homooligomer and the regulatory mechanism for Wnt signaling.
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