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Dynamic duo: Kir6 and SUR in KATP channel structure and function.
Patton, Bruce L; Zhu, Phillip; ElSheikh, Assmaa; Driggers, Camden M; Shyng, Show-Ling.
Afiliación
  • Patton BL; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR, USA.
  • Zhu P; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR, USA.
  • ElSheikh A; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR, USA.
  • Driggers CM; Department of Medical Biochemistry, Tanta University, Tanta, Egypt.
  • Shyng SL; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR, USA.
Channels (Austin) ; 18(1): 2327708, 2024 12.
Article en En | MEDLINE | ID: mdl-38489043
ABSTRACT
KATP channels are ligand-gated potassium channels that couple cellular energetics with membrane potential to regulate cell activity. Each channel is an eight subunit complex comprising four central pore-forming Kir6 inward rectifier potassium channel subunits surrounded by four regulatory subunits known as the sulfonylurea receptor, SUR, which confer homeostatic metabolic control of KATP gating. SUR is an ATP binding cassette (ABC) protein family homolog that lacks membrane transport activity but is essential for KATP expression and function. For more than four decades, understanding the structure-function relationship of Kir6 and SUR has remained a central objective of clinical significance. Here, we review progress in correlating the wealth of functional data in the literature with recent KATP cryoEM structures.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Potasio de Rectificación Interna Idioma: En Revista: Channels (Austin) Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Potasio de Rectificación Interna Idioma: En Revista: Channels (Austin) Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos