Postulated role of inter-domain interaction within the ryanodine receptor in Ca2+ channel regulation
Postulated role of inter-domain interaction within the ryanodine receptor in Ca2+ channel regulation
复制标题
DOI：
10.1016/s1050-1738(01)00067-6
复制
发表时间：
2000-10-01
影响因子：
9.3
通讯作者：
Yamamoto, T
中科院分区：
文献类型：
--
作者：
Ikemoto, N;Yamamoto, T
兴奋-收缩（E-C）偶联的关键步骤包括：（1）二氢吡啶（DHP）受体的激活剂部分（在骨骼肌中）的结合或通过DHP受体（在心肌中）进入的Ca 2+与兰尼碱受体（RyR）的结合，（2）RyR的整体蛋白质构象变化，以及（3）RyR Ca 2+通道的开放，导致肌肉收缩。构象变化（步骤2）在Ca 2+通道调节中起主要作用，并且许多“调节域”必须参与该过程。我们推测，这些调控结构域之间的相互作用是构象介导的Ca 2+通道控制的中心机制。在这篇综述中，我们总结了支持这一概念的最新数据。（Trends Endovasc Med 2000;10：310-316）。(C)2000年，Elsevier Science Inc.
Key steps of excitation-contraction (E-C) coupling ave (1) binding of the activator portion of the dihydropyridine (DHP) receptor (in skeletal muscle) or binding of the Ca2+ entered through the DHP receptor (in cardiac muscle) to the ryanodine receptor (RyR), (2) a global protein conformational change of the RyR, and (3) opening of the RyR Ca2+ channel, leading to muscle contraction. The conformational change (step 2) plays a major role in the Ca2+ channel regulation, and a number of "regulatory domains" must be involved in this process. We postulate that the interaction among these regulatory domains is the central mechanism for the conformation-mediated control of the Ca2+ channel. In this review, we summarize the recent data supporting this concept. (Trends Cardiovasc Med 2000;10:310-316). (C) 2000, Elsevier Science Inc.