Dynamic duo: Kir6 and SUR in K ATP channel structure and function.

Autor:	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.; Department of Medical Biochemistry, Tanta University, Tanta, Egypt., Driggers CM; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR, USA., Shyng SL; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, OR, USA.
Jazyk:	angličtina
Zdroj:	Channels (Austin, Tex.) [Channels (Austin)] 2024 Dec; Vol. 18 (1), pp. 2327708. Date of Electronic Publication: 2024 Mar 15.
DOI:	10.1080/19336950.2024.2327708
Abstrakt:	K ATP 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 K ATP gating. SUR is an ATP binding cassette (ABC) protein family homolog that lacks membrane transport activity but is essential for K ATP 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 K ATP cryoEM structures.
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu