期刊
JOURNAL OF NEUROSCIENCE
卷 26, 期 49, 页码 12727-12734出版社
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.2734-06.2006
关键词
prestin; OHC; electromotility; nonlinear capacitance; evolutionary trace; auditory
资金
- NIDCD NIH HHS [R01 DC000354, F32 DC000354, R01 DC000354-19, DC00354] Funding Source: Medline
- NIDDK NIH HHS [R90 DK071504-01, R90 DK071504] Funding Source: Medline
Prestin, a member of the SLC26A family of anion transporters, is a polytopic membrane protein found in outer hair cells (OHCs) of the mammalian cochlea. Prestin is an essential component of the membrane-based motor that enhances electromotility of OHCs and contributes to frequency sensitivity and selectivity in mammalian hearing. Mammalian cells expressing prestin display a nonlinear capacitance (NLC), widely accepted as the electrical signature of electromotility. The associated charge movement requires intracellular anions reflecting the membership of prestin in the SLC26A family. We used the computational approach of evolutionary trace analysis to identify candidate functional ( trace) residues in prestin for mutational studies. We created a panel of mutations at each trace residue and determined membrane expression and nonlinear capacitance associated with each mutant. Weobserve that several residue substitutions near the conserved sulfate transporter domain of prestin either greatly reduce or eliminate NLC, and the effect is dependent on the size of the substituted residue. These data suggest that packing of helices and interactions between residues surrounding the sulfate transporter motif is essential for normal prestin activity.
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