Abstract
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. copy; 2007 The Authors. Journal compilation
| Original language | English |
|---|---|
| Pages (from-to) | 451-461 |
| Number of pages | 11 |
| Journal | Journal of Physiology |
| Volume | 580 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 15 2007 |
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All Science Journal Classification (ASJC) codes
- Physiology
Cite this
Voltage-sensitive prestin orthologue expressed in zebrafish hair cells. / Albert, Jörg T.; Winter, Harald; Schaechinger, Thorsten J.; Weber, Thomas; Wang, Xiang; He, David Z.; Hendrich, Oliver; Geisler, Hyun Soon; Zimmermann, Ulrike; Oelmann, Katrin; Knipper, Marlies; Göpfert, Martin C.; Oliver, Dominik.
In: Journal of Physiology, Vol. 580, No. 2, 15.04.2007, p. 451-461.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Voltage-sensitive prestin orthologue expressed in zebrafish hair cells
AU - Albert, Jörg T.
AU - Winter, Harald
AU - Schaechinger, Thorsten J.
AU - Weber, Thomas
AU - Wang, Xiang
AU - He, David Z.
AU - Hendrich, Oliver
AU - Geisler, Hyun Soon
AU - Zimmermann, Ulrike
AU - Oelmann, Katrin
AU - Knipper, Marlies
AU - Göpfert, Martin C.
AU - Oliver, Dominik
PY - 2007/4/15
Y1 - 2007/4/15
N2 - 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. copy; 2007 The Authors. Journal compilation
AB - 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. copy; 2007 The Authors. Journal compilation
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U2 - 10.1113/jphysiol.2007.127993
DO - 10.1113/jphysiol.2007.127993
M3 - Article
C2 - 17272340
AN - SCOPUS:34147192135
VL - 580
SP - 451
EP - 461
JO - Journal of Physiology
JF - Journal of Physiology
SN - 0022-3751
IS - 2
ER -