Voltage-sensitive prestin orthologue expressed in zebrafish hair cells

被引:33
作者
Albert, Joerg 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
Goepfert, Martin C.
Oliver, Dominik [1 ]
机构
[1] Univ Freiburg, Inst Physiol 2, D-79104 Freiburg, Germany
[2] Creighton Univ, Sch Med, Dept Biomed Sci, Omaha, NE 68178 USA
[3] Univ Tubingen, Dept Otolaryngol, THRC, Mol Neurobiol Lab, D-72076 Tubingen, Germany
[4] Univ Cologne, Inst Zool, Volkswagen Fdn Res Grp, D-50923 Cologne, Germany
来源
JOURNAL OF PHYSIOLOGY-LONDON | 2007年 / 580卷 / 02期
关键词
D O I
10.1113/jphysiol.2007.127993
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
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 similar to 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.
引用
收藏
页码:451 / 461
页数:11
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