Center for Biomedical Engineering and Technology (BioMET), Department of Biochemistry and Molecular Biology, School of Medicine, University of Maryland, Baltimore, MD 21201, USA.
Cell Calcium. 2011 Oct;50(4):323-31. doi: 10.1016/j.ceca.2011.06.001. Epub 2011 Jul 23.
The release of Ca2+ ions from the sarcoplasmic reticulum through ryanodine receptor calcium release channels represents the critical step linking electrical excitation to muscular contraction in the heart and skeletal muscle (excitation-contraction coupling). Two small Ca2+ binding proteins, S100A1 and calmodulin, have been demonstrated to bind and regulate ryanodine receptor in vitro. This review focuses on recent work that has revealed new information about the endogenous roles of S100A1 and calmodulin in regulating skeletal muscle excitation-contraction coupling. S100A1 and calmodulin bind to an overlapping domain on the ryanodine receptor type 1 to tune the Ca2+ release process, and thereby regulate skeletal muscle function. We also discuss past, current and future work surrounding the regulation of ryanodine receptors by calmodulin and S100A1 in both cardiac and skeletal muscle, and the implications for excitation-contraction coupling.
肌浆网通过兰尼丁受体钙释放通道释放 Ca2+ 离子，这代表着将电兴奋与心脏和骨骼肌收缩（兴奋-收缩耦联）联系起来的关键步骤。两种小的 Ca2+ 结合蛋白，S100A1 和钙调蛋白，已被证明可在体外结合并调节兰尼丁受体。这篇综述重点介绍了最近的工作，这些工作揭示了 S100A1 和钙调蛋白在调节骨骼肌兴奋-收缩耦联中的内源性作用的新信息。S100A1 和钙调蛋白结合到兰尼丁受体 1 的重叠结构域上，以调节 Ca2+ 释放过程，从而调节骨骼肌功能。我们还讨论了围绕钙调蛋白和 S100A1 对心脏和骨骼肌中兰尼丁受体的调节的过去、现在和未来的工作，以及对兴奋-收缩耦联的影响。
