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XB-ART-3780
Science 2004 Mar 26;3035666:2007-10. doi: 10.1126/science.1093923.
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Actin polymerization-driven molecular movement of mDia1 in living cells.

Higashida C , Miyoshi T , Fujita A , Oceguera-Yanez F , Monypenny J , Andou Y , Narumiya S , Watanabe N .


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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.

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Species referenced: Xenopus
Genes referenced: actl6a fmn1 rho rho.2