Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin.

@article{McGuire2010CysteineMR,
  title={Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin.},
  author={R. Martin McGuire and Haiying Liu and Fred A Pereira and Robert M. Raphael},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 5},
  pages={3103-13}
}
The solute carrier transmembrane protein prestin (SLC26A5) drives an active electromechanical transduction process in cochlear outer hair cells that increases hearing sensitivity and frequency discrimination in mammals. A large intramembraneous charge movement, the nonlinear capacitance (NLC), is the electrical signature of prestin function. The transmembrane domain (TMD) helices and residues involved in the intramembrane charge displacement remain unknown. We have performed cysteine-scanning… CONTINUE READING
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