Evidence that prestin has at least two voltage-dependent steps

Kazuaki Homma*, Peter Dallos

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


Prestin is a voltage-dependent membrane-spanning motor protein that confers electromotility on mammalian cochlear outer hair cells, which is essential for normal hearing of mammals. Voltage-induced charge movement in the prestin molecule is converted into mechanical work; however, little is known about the molecular mechanism of this process. For understanding the electromechanical coupling mechanism of prestin, we simultaneously measured voltage-dependent charge movement and electromotility under conditions in which the magnitudes of both charge movement and electromotility are gradually manipulated by the prestin inhibitor, salicylate. We show that the observed relationships of the charge movement and the physical displacement (q-d relations) are well represented by a three-state Boltzmann model but not by a two-state model or its previously proposed variant. Here, we suggest a molecular mechanism of prestin with at least two voltage-dependent conformational transition steps having distinct electromechanical coupling efficiencies.

Original languageEnglish (US)
Pages (from-to)2297-2307
Number of pages11
JournalJournal of Biological Chemistry
Issue number3
StatePublished - Jan 21 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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