| Budget Amount *help |
¥40,040,000 (Direct Cost: ¥30,800,000、Indirect Cost: ¥9,240,000)
Fiscal Year 2016: ¥11,700,000 (Direct Cost: ¥9,000,000、Indirect Cost: ¥2,700,000)
Fiscal Year 2015: ¥19,630,000 (Direct Cost: ¥15,100,000、Indirect Cost: ¥4,530,000)
Fiscal Year 2014: ¥8,710,000 (Direct Cost: ¥6,700,000、Indirect Cost: ¥2,010,000)
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| Outline of Final Research Achievements |
The traction forces underlying cellular motility is regulated in part by the phosphorylation-induced modulation of coupling efficiency of the "clutch" molecule Shootin1 between F-actin and adhesion molecule L1-CAM, which bound the extracellular matrix. To establish the molecular basis of the regulatory mechanism, we analyzed by physical methods the structural and physical properties of Shootin1 and its physical interactions with L1-CAM and other regulatory proteins using purified protein samples. We found that three α-helical regions at the N-terminal half of Shootin1 and the phosphorylation sites existing at the first and second helical regions. The helical regions mediate Shootin1dimerization in solution and the phosphorylation at the N-terminal helical region induces formation of a tetramer or even higher oligomers to directly bind the cytoplasmic region of L1-CAM.
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