Han Dongju, Lim Younghyun, Lee Soah, Eyun Seong-Il
Department of Life Science, Chung-Ang University, Seoul, Korea.
Department of Biopharmaceutical Convergence, Sungkyunkwan University, Suwon, Korea.
Anim Cells Syst (Seoul). 2025 Jul 28;29(1):446-468. doi: 10.1080/19768354.2025.2533821. eCollection 2025.
The troponin complex is a critical component of thin filaments and plays an essential role in the calcium-mediated regulation of contraction and relaxation in striated muscles, including both cardiac and skeletal muscle. Troponin I, a subunit of this complex, inhibits actomyosin interactions during muscle relaxation. Its function is finely tuned by posttranslational modifications, particularly phosphorylation, which influence calcium sensitivity and actin affinity, thus impacting muscle contraction. Mutations in troponin I are closely associated with various human diseases. Specifically, several mutations in cardiac troponin I have been linked to cardiomyopathies, such as hypertrophic, dilated, and restrictive cardiomyopathies, which affect heart contractility and calcium handling. In this review, we explore the multifaceted aspects of troponin I, including its structure, functional role in muscle contraction, evolution, and the complex interactions between posttranslational modifications and genetic mutations that alter its function and contribute to disease progression.
肌钙蛋白复合体是细肌丝的关键组成部分，在包括心肌和骨骼肌在内的横纹肌的钙介导收缩和舒张调节中发挥着重要作用。肌钙蛋白I是该复合体的一个亚基，在肌肉舒张期间抑制肌动球蛋白相互作用。其功能通过翻译后修饰，特别是磷酸化进行精细调节，磷酸化会影响钙敏感性和肌动蛋白亲和力，从而影响肌肉收缩。肌钙蛋白I的突变与多种人类疾病密切相关。具体而言，心肌肌钙蛋白I的几种突变与心肌病有关，如肥厚型、扩张型和限制型心肌病，这些心肌病会影响心脏收缩力和钙处理。在这篇综述中，我们探讨了肌钙蛋白I的多方面内容，包括其结构、在肌肉收缩中的功能作用、进化，以及翻译后修饰和基因突变之间的复杂相互作用，这些相互作用会改变其功能并促进疾病进展。
