Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin.

@article{Cohen2005TwoDH,
  title={Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin.},
  author={Daniel M. Cohen and Hui Chen and Robert P. Johnson and Begum Choudhury and Susan W. Craig},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 17},
  pages={17109-17}
}
Vinculin is autoinhibited by an intramolecular interaction that masks binding sites for talin and F-actin. Although a recent structural model explains autoinhibition solely in terms of the interaction between vinculin tail (Vt) and residues 1-258 (D1), we find an absolute requirement for an interface involving the D4 domain of head (Vh residues 710-836) and Vt. Charge-to-alanine mutations in Vt revealed a class of mutants, T12 and T19, distal to the V-(1-258) binding site, which showed… CONTINUE READING