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

The Journal of Biological Chemistry
Makoto F KuwabaraKazuaki Homma

Abstract

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.

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Citations

May 6, 2019·Scientific Reports·Satoe TakahashiMary Ann Cheatham
Jun 26, 2020·Tissue Engineering. Part a·Rachel A HeuerAkihiro J Matsuoka
May 10, 2020·The Journal of General Physiology·Brenda FarrellWilliam E Brownell
Jul 28, 2020·Neural Plasticity·Zhongying WangZhiwu Huang
Jul 24, 2021·BMC Genomics·Zhongying WangZhiwu Huang
Jan 14, 2022·Nature Communications·Carmen ButanJoseph Santos-Sacchi

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