Voltage-sensitive prestin orthologue expressed in zebrafish hair cells

• Published in: The Journal of physiology Vol. 580; no. 2; pp. 451 - 461
• Main Authors: Albert, Jörg T., Winter, Harald, Schaechinger, Thorsten J., Weber, Thomas, Wang, Xiang, He, David Z. Z., Hendrich, Oliver, Geisler, Hyun‐Soon, Zimmermann, Ulrike, Oelmann, Katrin, Knipper, Marlies, Göpfert, Martin C., Oliver, Dominik
• Format: Journal Article
• Language: English
• Published: Oxford, UK The Physiological Society 15-04-2007; Blackwell Publishing Ltd; Blackwell Science Inc
• Subjects: Animals; Anion Transport Proteins - chemistry; Anion Transport Proteins - genetics; Anion Transport Proteins - metabolism; Cell Membrane - metabolism; Danio rerio; Electric Capacitance; Exons; Freshwater; Gene Expression; Hair Cells, Auditory - metabolism; Hair Cells, Auditory - physiology; Male; Molecular Structure; Neuroscience; Transfection; Zebrafish - genetics; Zebrafish - metabolism; Zebrafish - physiology; Zebrafish Proteins - chemistry; Zebrafish Proteins - genetics; Zebrafish Proteins - metabolism
• ISSN: 0022-3751; 1469-7793
• DOI: 10.1113/jphysiol.2007.127993

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.