Valvular dystrophy associated filamin A mutations reveal a new role of its first repeats in small-GTPase regulation.

@article{Duval2014ValvularDA,
  title={Valvular dystrophy associated filamin A mutations reveal a new role of its first repeats in small-GTPase regulation.},
  author={Damien Duval and Aur{\'e}lie Lardeux and Thierry le Tourneau and Russell A Norris and Roger R. Markwald and Vincent Sauzeau and Vincent Probst and Herv{\'e} Le Marec and Robert A. Levine and J J Schott and J. -L. M{\'e}rot},
  journal={Biochimica et biophysica acta},
  year={2014},
  volume={1843 2},
  pages={234-44}
}
Filamin A (FlnA) is a ubiquitous actin binding protein which anchors various transmembrane proteins to the cell cytoskeleton and provides a scaffold to many cytoplasmic signaling proteins involved in actin cytoskeleton remodeling in response to mechanical stress and cytokines stimulation. Although the vast majority of FlnA binding partners interact with the carboxy-terminal immunoglobulin like (Igl) repeats of FlnA, little is known on the role of the amino-N-terminal repeats. Here, using… CONTINUE READING