The structural basis of ryanodine receptor ion channel function

被引:162
作者
Meissner, Gerhard [1 ]
机构
[1] Univ N Carolina, Sch Med, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA
关键词
CALCIUM-RELEASE CHANNEL; MUSCLE SARCOPLASMIC-RETICULUM; RABBIT SKELETAL-MUSCLE; JUNCTIONAL TERMINAL CISTERNAE; CALMODULIN-BINDING SITES; SR CA2+ RELEASE; CARDIAC-MUSCLE; CA-2+ RELEASE; DIHYDROPYRIDINE RECEPTORS; SINGLE-CHANNEL;
D O I
10.1085/jgp.201711878
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
Large-conductance Ca2+ release channels known as ryanodine receptors (RyRs) mediate the release of Ca2+ from an intracellular membrane compartment, the endo/sarcoplasmic reticulum. There are three mammalian RyR iso-forms: RyR1 is present in skeletal muscle; RyR2 is in heart muscle; and RyR3 is expressed at low levels in many tissues including brain, smooth muscle, and slow-twitch skeletal muscle. RyRs form large protein complexes comprising four 560-kD RyR subunits, four similar to 12-kD FK506-binding proteins, and various accessory proteins including calmodulin, protein kinases, and protein phosphatases. RyRs share similar to 70% sequence identity, with the greatest sequence similarity in the C-terminal region that forms the transmembrane, ion-conducting domain comprising similar to 500 amino acids. The remaining similar to 4,500 amino acids form the large regulatory cytoplasmic "foot" structure. Experimental evidence for Ca2+, ATP, phosphorylation, and redox-sensitive sites in the cytoplasmic structure have been described. Exogenous effectors include the two Ca2+ releasing agents caffeine and ryanodine. Recent work describing the near atomic structures of mammalian skeletal and cardiac muscle RyRs provides a structural basis for the regulation of the RyRs by their multiple effectors.
引用
收藏
页码:1065 / 1089
页数:25
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