PUBLICATION
Voltage-sensitive prestin orthologue expressed in zebrafish hair cells
- Authors
- Albert, J.T., Winter, H., Schaechinger, T.J., Weber, T., Wang, X., He, D.Z., Hendrich, O., Geisler, H.S., Zimmermann, U., Oelmann, K., Knipper, M., Gopfert, M.C., and Oliver, D.
- ID
- ZDB-PUB-070212-24
- Date
- 2007
- Source
- The Journal of physiology 580(2): 451-461 (Journal)
- Registered Authors
- Weber, Thomas
- Keywords
- Auditory pathways
- MeSH Terms
-
- Animals
- Anion Transport Proteins/chemistry
- Anion Transport Proteins/genetics
- Anion Transport Proteins/metabolism*
- Cell Membrane/metabolism
- Electric Capacitance
- Exons
- Gene Expression
- Hair Cells, Auditory/metabolism*
- Hair Cells, Auditory/physiology
- Male
- Molecular Structure
- Transfection
- Zebrafish/genetics
- Zebrafish/metabolism*
- Zebrafish/physiology
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism*
- PubMed
- 17272340 Full text @ J. Physiol.
Citation
Albert, J.T., Winter, H., Schaechinger, T.J., Weber, T., Wang, X., He, D.Z., Hendrich, O., Geisler, H.S., Zimmermann, U., Oelmann, K., Knipper, M., Gopfert, M.C., and Oliver, D. (2007) Voltage-sensitive prestin orthologue expressed in zebrafish hair cells. The Journal of physiology. 580(2):451-461.
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 nonlinear capacitance (NLC) of the cell membrane. Compared to 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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping