Franzini-Armstrong C, Protasi F
Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, USA.
Physiol Rev. 1997 Jul;77(3):699-729. doi: 10.1152/physrev.1997.77.3.699.
The ryanodine receptor (RyR) is a high-conductance Ca2+ channel of the sarcoplasmic reticulum in muscle and of the endoplasmic reticulum in other cells. In striated muscle fibers, RyRs are responsible for the rapid release of Ca2+ that activates contraction. Ryanodine receptors are complex molecules, with unusually large cytoplasmic domains containing numerous binding sites for agents that control the state of activity of the channel-forming domain of the molecule. Structural considerations indicate that long-range interactions between cytoplasmic and intramembrane domains control channel function. Ryanodine receptors are located in specialized regions of the SR, where they are structurally and functionally associated with other intrinsic proteins and, indirectly, also with the luminal Ca2(+)-binding protein calsequestrin. Activation of RyRs during the early part of the excitation-contraction coupling cascade is initiated by the activity of surface-membrane Ca2+ channels, the dihydropyridine receptors (DHPRs). Skeletal and cardiac muscles contain different RyR and DHPR isoforms and both contribute to the diversity in cardiac and skeletal excitation-contraction coupling mechanisms. The architecture of the sarcoplasmic reticulum-surface junctions determines the types of RyR-DHPR interactions in the two muscle types.
兰尼碱受体(RyR)是肌肉中肌浆网以及其他细胞内质网中的一种高电导钙离子通道。在横纹肌纤维中,RyR负责钙离子的快速释放,从而激活收缩。兰尼碱受体是复杂的分子,具有异常大的胞质结构域,其中含有许多与控制分子通道形成结构域活性状态的因子结合的位点。结构上的考虑表明,胞质结构域和膜内结构域之间的远程相互作用控制着通道功能。兰尼碱受体位于肌浆网的特殊区域,在那里它们在结构和功能上与其他内在蛋白相关联,并且间接地也与腔内钙离子结合蛋白钙调蛋白相关联。在兴奋 - 收缩偶联级联反应的早期,RyR的激活是由表面膜钙离子通道——二氢吡啶受体(DHPR)的活性引发的。骨骼肌和心肌含有不同的RyR和DHPR同工型,两者都导致了心脏和骨骼肌兴奋 - 收缩偶联机制的多样性。肌浆网 - 表面连接的结构决定了两种肌肉类型中RyR - DHPR相互作用的类型。