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Originally published as Biophys J. BioFAST on March 24, 2006.
doi:10.1529/biophysj.105.073254
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Biophysical Journal 90:4035-4045 (2006)
© 2006 The Biophysical Society

An Anion Antiporter Model of Prestin, the Outer Hair Cell Motor Protein

Daniella Muallem and Jonathan Ashmore

Department of Physiology, University College London, London, United Kingdom

Correspondence: Address reprint requests to Jonathan Ashmore, Dept. of Physiology, UCL, Gower St., London WC1E 6BT UK. Tel.: 44-207-679-6080; E-mail: j.ashmore{at}ucl.ac.uk.

Cochlear amplification in mammalian hearing relies on an active mechanical feedback process generated by outer hair cells, driven by a protein, prestin (SLC26A5), in the lateral membrane. We have used kinetic models to understand the mechanism by which prestin might function. We show that the two previous hypotheses of prestin, which assume prestin cannot operate as a transporter, are insufficient to explain previously published data. We propose an alternative model of prestin as an electrogenic anion exchanger, exchanging one Cl– ion for one divalent or two monovalent anions. This model can reproduce the key aspects of previous experimental observations. The experimentally observed charge movements are produced by the translocation of one Cl– ion combined with intrinsic positively charged residues, while the transport of the counteranion is electroneutral. We tested the model with measurements of the Cl– dependence of charge movement, using Formula to replace Cl–. The data was compatible with the predictions of the model, suggesting that prestin does indeed function as a transporter.




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