Structural and physical properties of the clutch molecular complex in motile cells.

2017 Fiscal Year Final Research Report

• Project/Area Number: 26251006
• Research Category: Grant-in-Aid for Scientific Research (A)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Nara Institute of Science and Technology
• Principal Investigator: Hakoshima Toshio 奈良先端科学技術大学院大学, バイオサイエンス研究科, 教授 (00164773)
• Co-Investigator(Kenkyū-buntansha): 稲垣 直之 奈良先端科学技術大学院大学, バイオサイエンス研究科, 教授 (20223216)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: 構造生物学 / 生化学 / 生物物理学 / 分子細胞生物学 / タンパク質 / 相互作用 / 構造変化 / 制御機構

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.

Free Research Field

構造生物学