The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization.

@article{Shimada2004TheCF,
  title={The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization.},
  author={Atsushi Shimada and Mikl{\'o}s Nyitrai and Ingrid R. Vetter and Dorothee K{\"u}hlmann and Be{\'a}ta Bugyi and Shuh Narumiya and Michael A. Geeves and Alfred Wittinghofer},
  journal={Molecular cell},
  year={2004},
  volume={13 4},
  pages={511-22}
}
Diaphanous-related formins (Drf) are activated by Rho GTP binding proteins and induce polymerization of unbranched actin filaments. They contain three formin homology domains. Evidence as to the effect of formins on actin polymerization were obtained using FH2/FH1 constructs of various length from different Drfs. Here we define the core FH2 domain as a proteolytically stable domain of approximately 338 residues. The monomeric FH2 domains from mDia1 and mDia3 inhibit polymerization of actin and… CONTINUE READING