Control of Slc7a5 sensitivity by the voltage-sensing domain of Kv1 channels

• DOI: 10.7554/elife.54916
• Publication Date: 2020-11-09T13:01:26Z
• Authors: Shawn M Lamothe; Nazlee Sharmin; Grace Silver; Motoyasu Satou; Yubin Hao; Toru Tateno; Victoria A Baronas; Harley T Kurata
• Keywords: Disinhibition; HEK 293 cells

Many voltage-dependent ion channels are regulated by accessory proteins. We recently reported powerful regulation of Kv1.2 potassium the amino acid transporter Slc7a5. In this study, we report that Kv1.1 also Slc7a5, albeit with different functional outcomes. heterologous expression systems, exhibits prominent current enhancement ('disinhibition') holding potentials more negative than −120 mV. Knockdown endogenous Slc7a5 leads to larger currents and strongly attenuates disinhibition effect, suggesting involves channel inhibition can be reversed supraphysiological hyperpolarizing voltages. investigated chimeric combinations Kv1.2, demonstrating exchange voltage-sensing domain controls sensitivity response localize a specific position in S1 effects on sensitivity. Overall, our study highlights multiple Slc7a5-sensitive Kv1 subunits, identifies as determinant modulation channels.