Mutation-induced reinforcement of prestin-expressing cells

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

doi:10.1016/j.bbrc.2009.09.016

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

Otolaryngology

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	569-574
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	389
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2009.09.016
State	Published - Nov 27 2009

Funding

This work was supported by Grant-in-Aid for Scientific Research (B) 18390455 from the Japan Society for the Promotion of Science , by Grant-in-Aid for Exploratory Research 18659495 from the Ministry of Education, Culture, Sports, Science and Technology of Japan , by a grant from the Human Frontier Science Program, by a Health and Labour Science Research Grant from the Ministry of Health, Labour and Welfare of Japan and by Tohoku University Global COE Program “Global Nano-Biomedical Engineering Education and Research Network Centre” to H.W., and by a Grant-in-Aid for JSPS Fellows from the Japan Society for the Promotion of Science to S.K.

Keywords

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

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
Cell Biology

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10.1016/j.bbrc.2009.09.016

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title = "Mutation-induced reinforcement of prestin-expressing cells",

abstract = "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.",

keywords = "Electrophysiological property, Inner ear, Outer hair cell, Point mutation, Prestin, Somatic motility",

author = "Shun Kumano and Xiaodong Tan and He, {David Z Z} and Koji Iida and Michio Murakoshi and Hiroshi Wada",

note = "Funding Information: This work was supported by Grant-in-Aid for Scientific Research (B) 18390455 from the Japan Society for the Promotion of Science , by Grant-in-Aid for Exploratory Research 18659495 from the Ministry of Education, Culture, Sports, Science and Technology of Japan , by a grant from the Human Frontier Science Program, by a Health and Labour Science Research Grant from the Ministry of Health, Labour and Welfare of Japan and by Tohoku University Global COE Program “Global Nano-Biomedical Engineering Education and Research Network Centre” to H.W., and by a Grant-in-Aid for JSPS Fellows from the Japan Society for the Promotion of Science to S.K.",

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T1 - Mutation-induced reinforcement of prestin-expressing cells

AU - Kumano, Shun

AU - Tan, Xiaodong

AU - He, David Z Z

AU - Iida, Koji

AU - Murakoshi, Michio

AU - Wada, Hiroshi

N1 - Funding Information: This work was supported by Grant-in-Aid for Scientific Research (B) 18390455 from the Japan Society for the Promotion of Science , by Grant-in-Aid for Exploratory Research 18659495 from the Ministry of Education, Culture, Sports, Science and Technology of Japan , by a grant from the Human Frontier Science Program, by a Health and Labour Science Research Grant from the Ministry of Health, Labour and Welfare of Japan and by Tohoku University Global COE Program “Global Nano-Biomedical Engineering Education and Research Network Centre” to H.W., and by a Grant-in-Aid for JSPS Fellows from the Japan Society for the Promotion of Science to S.K.

PY - 2009/11/27

Y1 - 2009/11/27

N2 - 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.

AB - 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.

KW - Electrophysiological property

KW - Inner ear

KW - Outer hair cell

KW - Point mutation

KW - Prestin

KW - Somatic motility

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Mutation-induced reinforcement of prestin-expressing cells

Abstract

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Keywords

ASJC Scopus subject areas

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