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首页> 外文期刊>Cytoskeleton >Sarcomeric and nonmuscle α‐actinin isoforms exhibit differential dynamics at skeletal muscle Z Z ‐lines
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Sarcomeric and nonmuscle α‐actinin isoforms exhibit differential dynamics at skeletal muscle Z Z ‐lines

机译：Sarcomeric和Nonmuscleα-肌动蛋白同种型在骨骼肌Z Z -Lines上表现出差分动力学

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Abstract The α‐actinin proteins are a highly conserved family of actin crosslinkers that mediate interactions between several cytoskeletal and sarcomeric proteins. Nonsarcomeric α‐actinin‐1 and α‐actinin‐4 crosslink actin filaments in the cytoskeleton, while sarcomeric α‐actinin‐2 and α‐actinin‐3 serve a crucial role in anchoring actin filaments to the muscle Z‐line. To assess the difference in turnover dynamics and structure/function properties between the α‐actinin isoforms at the sarcomeric Z‐line, we used Fluorescence Recovery After Photobleaching (FRAP) in primary myofiber cultures. We found that the recovery kinetics of these proteins followed three distinct patterns: α‐actinin‐2/α‐actinin‐3 had the slowest turn over, α‐actinin‐1 recovered to an intermediate degree, and α‐actinin‐4 had the fastest recovery. Interestingly, the isoforms’ patterns of recovery were reversed at adhesion plaques in fibroblasts. This disparity suggests that the different α‐actinin isoforms have unique association kinetics in myofibers and that nonmuscle isoform interactions are more dynamic at the sarcomeric Z‐line. Protein domain‐specific investigations using α‐actinin‐2/4 chimeric proteins showed that differential dynamics between sarcomeric and nonmuscle isoforms are regulated by cooperative interactions between the N‐terminal actin‐binding domain, the spectrin‐like linker region and the C‐terminal calmodulin‐like EF hand domain. Together, these findings demonstrate that α‐actinin isoforms are unique in binding dynamics at the Z‐line and suggest differentially evolved interactive and Z‐line association capabilities of each functional domain.
机译：摘要α-肌醇蛋白蛋白是一种高度保守的肌动蛋白交联剂系列，其介导几种细胞骨骼和肉瘤蛋白之间的相互作用。非甘蓝型α-肌醇蛋白-1和α-肌动蛋白-4交联肌肽细胞蛋白在细胞骨架中，而SARCOMERORERα-肌醇蛋白-2和α-肌醇蛋白-3在将肌动蛋白长丝锚固到肌肉Z线上的关键作用。为了评估Sarcomeric Z-Line的α-挥发蛋白同种型之间的营种动力学和结构/功能性质的差异，我们在原发性二手纤维培养物中使用光漂白（FRAP）后的荧光回收。我们发现这些蛋白质的回收动力学跟随三个不同的图案：α-肌醇素-2 /α-肌动蛋白-3具有最慢的翻转，α-肌醇素-1回收到中间度，α-肌醇蛋白-4具有最快的恢复。有趣的是，同种型的复苏模式在成纤维细胞中的粘附斑块中逆转。这种差异表明，不同的α-肌动蛋白同种型在肌纤维中具有独特的关联动力学，并且非用途同种型相互作用在SARComeric Z线上更具动态。使用α-肌醇蛋白-2 / 4嵌合蛋白的蛋白质结构域的特异性研究表明，通过N-末端肌动蛋白结合结构域，光谱样接头区域和C末端之间的协同相互作用来调节SARCOMERIC和非肌肉同种型之间的差动动力学钙调蛋白样EF手领域。这些发现在一起表明α-肌醇蛋白同种型在Z线处的结合动力学中是独特的，并且表达每个功能域的差异演化的交互和Z线关联能力。

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