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Article

Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin.

The Journal of biological chemistry - 29 Jan 2010

McGuire Ryan M, Liu Haiying, Pereira Fred A, Raphael Robert M

Abstract excerpt

The solute carrier transmembrane protein prestin (SLC26A5) drives an active electromechanical transduction process in cochlear outer hair cells that increases hearing sensitivity and frequency discrimination in mammals. A large intramembraneous charge movement, the nonlinear capacitance (NLC), is the electrical signature of prestin function. The transmembrane domain (TMD) helices and residues involved in the...

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Identifiers

PMID: 19926791
DOI: 10.1074/jbc.M109.053249
PMCID: PMC2823402

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin.PMID 19926791Read ↗

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The frequency dependence of prestin-mediated fast electromotility for mammalian cochlear amplificationSemantic proximity Read ↗

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The R130S mutation significantly affects the function of prestin, the outer hair cell motor protein.Semantic proximity Read ↗

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