Mechanosignaling pathways alter muscle structure and function by post-translational modification of existing sarcomeric proteins to optimize energy usage.
Mechanosignaling pathways alter muscle structure and function by post-translational modification of existing sarcomeric proteins to optimize energy usage.
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机械信号通路通过现有肌节蛋白的翻译后修饰来改变肌肉结构和功能，以优化能量利用。
DOI：
10.1007/s10974-021-09596-9
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发表时间：
2021-06
影响因子：
2.7
通讯作者：
Solís C
中科院分区：
文献类型：
--
作者：
Russell B;Solís C
传导的机械信号到达肌肉的目的地改变了肌节的结构和功能。解决的一个主要问题是如何优化肌肉质量和张力生成，以满足实际的性能需求，使很少的能量被浪费。三种情况下，提高能源效率的检查：肌钙蛋白复合物的调谐力生产，控制肌球蛋白头在休息状态，和Z盘蛋白肌节组装。蛋白质复合物的调节通常由翻译后修饰（PTM）控制，其中最常见的是激酶的磷酸化，组蛋白脱乙酰酶的脱乙酰化和E3连接酶的泛素化。信号的另一个分支不通过肽共价键而通过配体相互作用（例如Ca 2+和磷酸肌醇结合）起作用。肌球蛋白头部和肌钙蛋白复合物对其与肌动蛋白结合的调节是改变肌原纤维收缩性的信号终点的最好和最早的例子。肌钙蛋白复合物中的PTM通过蛋白质降解调节收缩功能的效率以匹配对工作的生理需求和肌肉质量。肌节组装的调节，通过整合传入的信号通路，导致相同的PTM或配体结合的Z盘蛋白CapZ，α-辅肌动蛋白，telethonin，肌联蛋白N-末端，和其他人的机械加载和卸载进行了讨论。许多导致心肌病和心脏病的人类突变发生在上述蛋白质中，这些蛋白质通常发生在它们的PTM或配体结合位点。
A transduced mechanical signal arriving at its destination in muscle alters sarcomeric structure and function. A major question addressed is how muscle mass and tension generation are optimized to match actual performance demands so that little energy is wasted. Three cases for improved energy efficiency are examined: the troponin complex for tuning force production, control of the myosin heads in a resting state, and the Z-disc proteins for sarcomere assembly. On arrival, the regulation of protein complexes is often controlled by post-translational modification (PTM), of which the most common are phosphorylation by kinases, deacetylation by histone deacetylases and ubiquitination by E3 ligases. Another branch of signals acts not through peptide covalent bonding but via ligand interactions (e.g. Ca2+ and phosphoinositide binding). The myosin head and the regulation of its binding to actin by the troponin complex is the best and earliest example of signal destinations that modify myofibrillar contractility. PTMs in the troponin complex regulate both the efficiency of the contractile function to match physiologic demand for work, and muscle mass via protein degradation. The regulation of sarcomere assembly by integration of incoming signaling pathways causing the same PTMs or ligand binding are discussed in response to mechanical loading and unloading by the Z-disc proteins CapZ, α-actinin, telethonin, titin N-termini, and others. Many human mutations that lead to cardiomyopathy and heart disease occur in the proteins discussed above, which often occur at their PTM or ligand binding sites.
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影响因子：
56.9
作者：
Choudhary, Chunaram;Kumar, Chanchal;Mann, Matthias
通讯作者：
Mann, Matthias
影响因子：
3.7
作者：
Foster DB;Liu T;Rucker J;O'Meally RN;Devine LR;Cole RN;O'Rourke B
通讯作者：
O'Rourke B
影响因子：
3.6
作者：
EISENBERG, BR;SALMONS, S
通讯作者：
SALMONS, S
活着的心脏成纤维细胞和心肌细胞中荧光标记的脑和肌肉肌动蛋白的相同分布。
DOI：
10.1083/jcb.100.1.292
发表时间：
1985-01
期刊：
The Journal of cell biology
影响因子：
--
作者：
McKenna N;Meigs JB;Wang YL
通讯作者：
Wang YL
影响因子：
2.9
作者：
COOPER, JA;POLLARD, TD
通讯作者：
POLLARD, TD