mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells

Sadanori Watanabe, Yoshikazu Ando, Shingo Yasuda, Hiroshi Hosoya, Naoki Watanabe, Toshimasa Ishizaki, Shuh Narumiya

    Research output: Contribution to journalArticlepeer-review

    132 Citations (Scopus)

    Abstract

    mDia proteins are mammalian homologues of Drosophila diaphanous and belong to the formin family proteins that catalyze actin nucleation and polymerization. Although formin family proteins of nonmammalian species such as Drosophila diaphanous are essential in cytokinesis, whether and how mDia proteins function in cytokinesis remain unknown. Here we depleted each of the three mDia isoforms in NIH 3T3 cells by RNA interference and examined this issue. Depletion of mDia2 selectively increased the number of binucleate cells, which was corrected by coexpression of RNAi-resistant full-length mDia2. mDia2 accumulates in the cleavage furrow during anaphase to telophase, and concentrates in the midbody at the end of cytokinesis. Depletion of mDia2 induced contraction at aberrant sites of dividing cells, where contractile ring components such as RhoA, myosin, anillin, and phosphorylated ERM accumulated. Treatment with blebbistatin suppressed abnormal contraction, corrected localization of the above components, and revealed that the amount of F-actin at the equatorial region during anaphase/telophase was significantly decreased with mDia2 RNAi. These results demonstrate that mDia2 is essential in mammalian cell cytokinesis and that mDia2-induced F-actin forms a scaffold for the contractile ring and maintains its position in the middle of a dividing cell.

    Original languageEnglish
    Pages (from-to)2328-2338
    Number of pages11
    JournalMolecular biology of the cell
    Volume19
    Issue number5
    DOIs
    Publication statusPublished - 2008 May 1

    ASJC Scopus subject areas

    • Molecular Biology
    • Cell Biology

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