Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation

@article{Pernier2013DimericWD,
  title={Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation},
  author={Julien Pernier and J{\'o}zsef Orb{\'a}n and Balendu Sankara Avvaru and Antoine Jegou and Guillaume Romet-Lemonne and B{\'e}reng{\`e}re Guichard and M. Carlier},
  journal={Nature Structural &Molecular Biology},
  year={2013},
  volume={20},
  pages={1069-1076}
}
Proteins containing repeats of the WASP homology 2 (WH2) actin-binding module are multifunctional regulators of actin nucleation and assembly. The bacterial effector VopF in Vibrio cholerae, like VopL in Vibrio parahaemolyticus, is a unique homodimer of three WH2 motifs linked by a C-terminal dimerization domain. We show that only the first and third WH2 domains of VopF bind G-actin in a non-nucleating, sequestered conformation. Moreover, dimeric WH2 domains in VopF give rise to unprecedented… CONTINUE READING