Mutation-induced reinforcement of prestin-expressing cells

Shun Kumano, Xiaodong Tan, David Z Z He, Koji Iida, Michio Murakoshi, Hiroshi Wada*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The motor protein prestin in cochlear outer hair cells is a member of the solute carrier 26 family, but among the proteins of that family, only prestin can confer the cells with nonlinear capacitance (NLC) and motility. In the present study, to clarify contributions of unique amino acids of prestin, namely, Met-122, Met-225 and Thr-428, to the characteristics of prestin, mutations were introduced into those amino acids. As a result, NLC remained unchanged by both replacement of Met-122 by isoleucine and that of Thr-428 by leucine, suggesting that those amino acids were not important for the generation of NLC. Surprisingly, the replacement of Met-225 by glutamine statistically increased NLC as well as the motility of prestin-expressing cells without an increase in the amount of prestin expression in the plasma membrane. This indicates that Met-225 in prestin somehow adjusts NLC and the motility of prestin-expressing cells.

Original languageEnglish (US)
Pages (from-to)569-574
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Nov 27 2009


  • Electrophysiological property
  • Inner ear
  • Outer hair cell
  • Point mutation
  • Prestin
  • Somatic motility

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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