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This Article Full Text Full Text (PDF) All Versions of this Article: 580/2/451    most recent jphysiol.2007.127993v1 Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Albert, J. T. Articles by Oliver, D. Search for Related Content PubMed PubMed Citation Articles by Albert, J. T. Articles by Oliver, D. Related Collections Neuroscience

¹ Volkswagen Foundation Research Group, Institute of Zoology, University of Cologne, 50923 Cologne, Germany
² University of Tübingen, Department of Otolaryngology, Tübingen Hearing Research Centre (THRC), Laboratory of Molecular Neurobiology, Elfriede-Aulhorn-Straße 5, D-72076 Tübingen, 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

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 non-linear capacitance (NLC) of the cell membrane. Compared with 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.

(Received 10 January 2007; accepted after revision 25 January 2007; first published online 1 February 2007)
Corresponding author D. Oliver:  Email: dominik.oliver{at}physiologie.uni-freiburg.de, Also: m.gopfert{at}uni-koeln.de and marlies.knipper{at}uni-tuebingen.de

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