Actin Polymerization-Driven Molecular Movement of mDia1 in Living Cells

Chiharu Higashida, Takushi Miyoshi, Akiko Fujita, Fabian Oceguera-Yanez, James Monypenny, Yoshikazu Andou, Shuh Narumiya, Naoki Watanabe

    Research output: Contribution to journalArticlepeer-review

    235 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)2007-2010
    Number of pages4
    JournalScience
    Volume303
    Issue number5666
    DOIs
    Publication statusPublished - 2004 Mar 26

    ASJC Scopus subject areas

    • General

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