The extracellular loop of pendrin and prestin modulates their voltage-sensing property

Makoto F. Kuwabara, Koichiro Wasano, Satoe Takahashi, Justin Bodner, Tomotaka Komori, Sotaro Uemura, Jing Zheng, Tomohiro Shima, Kazuaki Homma*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Pendrin and prestin belong to the solute carrier 26 (SLC26) family of anion transporters. Prestin is unique among the SLC26 family members in that it displays voltage-driven motor activity (electromotility) and concurrent gating currents that manifest as nonlinear cell membrane electrical capacitance (nonlinear capacitance (NLC)). Although the anion transport mechanism of the SLC26 proteins has begun to be elucidated, the molecular mechanism of electromotility, which is thought to have evolved from an ancestral ion transport mechanism, still remains largely elusive. Here, we demonstrate that pendrin also exhibits large NLC and that charged residues present in one of the extracellular loops of pendrin and prestin play significant roles in setting the voltage-operating points of NLC. Our results suggest that the molecular mechanism responsible for sensing voltage is not unique to prestin among the members of the SLC26 family and that this voltage-sensing mechanism works independently of the anion transport mechanism.

Original languageEnglish (US)
Pages (from-to)9970-9980
Number of pages11
JournalJournal of Biological Chemistry
Issue number26
StatePublished - Jun 29 2018

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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