Single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells, which was blocked by actin-perturbing drugs.
The study demonstrates that mDia1 moves processively along the growing end of actin filaments, suggesting Formins may act as molecular motility machinery independent of motor proteins.
mDia1, a Rho effector, belongs to the Formin family of proteins, which shares the conserved tandem FH1-FH2 unit structure. Formins including mDia1 accelerate actin nucleation while interacting with actin filament fast-growing ends. Here our single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells. The movement of mDia1 FH1-FH2 was blocked by actin-perturbing drugs, and the speed of mDia1 FH1-FH2 movement appeared to correlate with actin elongation rates. In vitro, mDia1 FH1-FH2 associated persistently with the growing actin barbed end. mDia1 probably moves processively along the growing end of actin filaments in cells, and Formins may be a molecular motility machinery that is independent from motor proteins.
Higashida et al. (2004) studied Living cells. mDia1 FH1-FH2 was evaluated on Molecular movement of mDia1. Single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells, which was blocked by actin-perturbing drugs.