Department of Physiology, Wayne State University School of Medicine, 540 E. Canfield, Detroit, MI, 48201, USA.
Department of Physiology, Wayne State University School of Medicine, 540 E. Canfield, Detroit, MI, 48201, USA.
Arch Biochem Biophys. 2019 May 15;666:40-45. doi: 10.1016/j.abb.2019.03.013. Epub 2019 Mar 27.
The troponin complex plays a central role in regulating the contraction and relaxation of striated muscles. Among the three protein subunits of troponin, the calcium receptor subunit, TnC, belongs to the calmodulin family of calcium signaling proteins whereas the inhibitory subunit, TnI, and tropomyosin-binding/thin filament-anchoring subunit, TnT, are striated muscle-specific regulatory proteins. TnI and TnT emerged early in bilateral symmetric invertebrate animals and have co-evolved during the 500-700 million years of muscle evolution. To understand the divergence as well as conservation of the structures of TnI and TnT in invertebrate and vertebrate organisms adds novel insights into the structure-function relationship of troponin and the muscle type isoforms of TnI and TnT. Based on the significant growth of genomic database of multiple species in the past decade, this focused review studied the primary structure features of invertebrate troponin subunits in comparisons with the vertebrate counterparts. The evolutionary data demonstrate valuable information for a better understanding of the thin filament regulation of striated muscle contractility in health and diseases.
肌钙蛋白复合物在调节横纹肌的收缩和松弛中起着核心作用。在肌钙蛋白的三个蛋白亚基中,钙受体亚基 TnC 属于钙信号蛋白的钙调蛋白家族,而抑制亚基 TnI 和原肌球蛋白结合/细肌丝锚定亚基 TnT 是横纹肌特异性调节蛋白。TnI 和 TnT 早在双侧对称的无脊椎动物中出现,并在 5 亿至 7 亿年的肌肉进化过程中共同进化。了解无脊椎动物和脊椎动物生物中 TnI 和 TnT 结构的差异和保守性,为肌钙蛋白的结构-功能关系以及 TnI 和 TnT 的肌肉亚型提供了新的见解。基于过去十年多种物种基因组数据库的显著增长,本综述重点研究了与脊椎动物相比无脊椎动物肌钙蛋白亚基的一级结构特征。进化数据为更好地理解健康和疾病状态下横纹肌收缩性的细肌丝调节提供了有价值的信息。