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Voltage‐sensitive prestin orthologue expressed in zebrafish hair cells
Author(s) -
Albert Jörg T.,
Winter Harald,
Schaechinger Thorsten J.,
Weber Thomas,
Wang Xiang,
He David Z. Z.,
Hendrich Oliver,
Geisler HyunSoon,
Zimmermann Ulrike,
Oelmann Katrin,
Knipper Marlies,
Göpfert Martin C.,
Oliver Dominik
Publication year - 2007
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2007.127993
Subject(s) - prestin , motor protein , zebrafish , hair cell , microbiology and biotechnology , chemistry , biology , patch clamp , biophysics , biochemistry , cochlea , electrophysiology , gene , neuroscience , microtubule
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.