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Control of Slc7a5 sensitivity by the voltage-sensing domain of Kv1 channels.
Lamothe, Shawn M; Sharmin, Nazlee; Silver, Grace; Satou, Motoyasu; Hao, Yubin; Tateno, Toru; Baronas, Victoria A; Kurata, Harley T.
Afiliación
  • Lamothe SM; Department of Pharmacology, Alberta Diabetes Institute, University of Alberta, Edmonton, Canada.
  • Sharmin N; School of Dentistry, Faculty of Medicine and Dentistry, University of Alberta, School of Dentistry, Edmonton Clinic Health Academy (ECHA), Edmonton, Canada.
  • Silver G; Department of Pharmacology, Alberta Diabetes Institute, University of Alberta, Edmonton, Canada.
  • Satou M; Department of Biochemistry, Dokkyo Medical University School of Medicine, Tochigi, Japan.
  • Hao Y; Department of Medicine, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Canada.
  • Tateno T; Department of Pharmacology, Alberta Diabetes Institute, University of Alberta, Edmonton, Canada.
  • Baronas VA; Department of Medicine, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Canada.
  • Kurata HT; Department of Pharmacology, Alberta Diabetes Institute, University of Alberta, Edmonton, Canada.
Elife ; 92020 11 09.
Article en En | MEDLINE | ID: mdl-33164746
Many voltage-dependent ion channels are regulated by accessory proteins. We recently reported powerful regulation of Kv1.2 potassium channels by the amino acid transporter Slc7a5. In this study, we report that Kv1.1 channels are also regulated by Slc7a5, albeit with different functional outcomes. In heterologous expression systems, Kv1.1 exhibits prominent current enhancement ('disinhibition') with holding potentials more negative than -120 mV. Knockdown of endogenous Slc7a5 leads to larger Kv1.1 currents and strongly attenuates the disinhibition effect, suggesting that Slc7a5 regulation of Kv1.1 involves channel inhibition that can be reversed by supraphysiological hyperpolarizing voltages. We investigated chimeric combinations of Kv1.1 and Kv1.2, demonstrating that exchange of the voltage-sensing domain controls the sensitivity and response to Slc7a5, and localize a specific position in S1 with prominent effects on Slc7a5 sensitivity. Overall, our study highlights multiple Slc7a5-sensitive Kv1 subunits, and identifies the voltage-sensing domain as a determinant of Slc7a5 modulation of Kv1 channels.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transportador de Aminoácidos Neutros Grandes 1 / Canal de Potasio Kv.1.1 Tipo de estudio: Diagnostic_studies Límite: Animals / Humans Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transportador de Aminoácidos Neutros Grandes 1 / Canal de Potasio Kv.1.1 Tipo de estudio: Diagnostic_studies Límite: Animals / Humans Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Reino Unido