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

@article{Watanabe2008mDia2IT,
  title={mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells.},
  author={Sadanori Watanabe and Yoshikazu Ando and Shingo Yasuda and Hiroshi Hosoya and Naoki Watanabe and Toshimasa Ishizaki and Shuh Narumiya},
  journal={Molecular biology of the cell},
  year={2008},
  volume={19 5},
  pages={
          2328-38
        }
}
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… CONTINUE READING