The actin filament system is universal throughout eukaryotes, and actin polymerization facilitates cell locomotion, morphogenesis and cell-to-cell interactions. The formin family, the molecules that accelerate actin polymerization, has been known for their ability to move rapidly over the long distance by continuously binding the tip of the polymerizing actin filament. This ability was discovered in the previous study using live-cell fluorescence single-molecule imaging conducted by the research group led by Professor Naoki Watanabe at Tohoku University Graduate School of Life Sciences (published in Science in 2004). A new study by the same group has now elucidated that mDia1, a member of the formin family, rotates along the double helical structure of the actin filament while it elongates an actin filament. This finding implies a new mechanism of cytoskeletal polymer regulation through the interaction between the force generated by actin polymerization and the torsional stress stored in actin filaments.
   
 These research results were discovered by Professor Naoki Watanabe and Hiroaki Mizuno, a postdoctoral researcher at Tohoku University Graduate School of Life Sciences in collaboration with Kyoto University Faculty of Medicine, and have been published online in Science on December 9, 2010 （http://www.sciencexpress.org）.

More Information (Japanese)

[Contact information]
Professor Naoki Watanabe
Tohoku University Graduate School of Life Sciences
TEL&FAX: +81-22-795-6693
E-mail: nwatanabe*m.tohoku.ac.jp (Replace * with @)