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Received January 10, 2007
Revised January 15, 2007
Accepted after revision January 25, 2007
1 Volkswagen Foundation Research Group, Institute of Zoology, University of Cologne, Germany
2 University of Tuebingen, Tuebingen Hearing Research Centre (THRC), Germany
3 Institute of Physiology II, University of Freiburg, 79104 Freiburg, Germany
4 Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE, 68178, USA
* To whom correspondence should be addressed. E-mail: joerg.albert{at}uni-koeln.de.
Prestin, a member of the solute carrier (SLC) family SLC26A, is the molecular motor that drives the somatic electromotility of mammalian outer hair cells (OHCs). Its closest reported homologue, zebrafish prestin (zprestin), shares ~70% strong amino acid sequence similarity with mammalian prestin, predicting an almost identical protein structure. Immunohistochemical analysis now shows that zprestin is expressed in hair cells of the zebrafish ear. Similar to mammalian prestin, heterologously expressed zprestin is found to generate voltage dependent charge movements, giving rise to a nonlinear capacitance (NLC) of the cell membrane. Compared to mammalian prestin, charge movements mediated by zprestin display a weaker voltage dependence and slower kinetics; they occur at more positive membrane voltages, and are not associated with electromotile responses. Given this functional dissociation of NLC and electromotility and the structural similarity with mammalian prestin, we anticipate that zprestin provides a valuable tool for tracing the molecular and evolutionary bases of prestin motor function.
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