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首页> 外文期刊>Journal of Muscle Research and Cell Motility >Myopodin is an F-actin bundling protein with multiple independent actin-binding regions
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Myopodin is an F-actin bundling protein with multiple independent actin-binding regions

机译：Myopodin是一种F-肌动蛋白捆绑蛋白，具有多个独立的肌动蛋白结合区

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摘要

The assembly of striated muscle myofibrils is a multistep process in which a variety of proteins is involved. One of the first and most important steps in myofibrillogenesis is the arrangement of thin myofilaments into ordered I-Z-I brushes, requiring the coordinated activity of numerous actin binding proteins. The early expression of myopodin prior to sarcomeric α-actinin, as well as its binding to actin, α-actinin and filamin indicate an important role for this protein in actin cytoskeleton remodelling with the precise function of myopodin in this process yet remaining to be resolved. While myopodin was previously described as a protein capable of cross-linking actin filaments into thick bundles upon transient transfections, it has remained unclear whether myopodin alone is capable of bundling actin, or if additional proteins are involved. We have therefore investigated the in vitro actin binding properties of myopodin. High speed cosedimentation assays with skeletal muscle actin confirmed direct binding of myopodin to F-actin and showed that this interaction is mediated by at least two independent actin binding sites, found in all myopodin isoforms identified to date. Furthermore, low-speed cosedimentation assays revealed that not only full length myopodin, but also the fragment containing only the second binding site, bundles microfilaments in the absence of accessory proteins. Ultrastructural analysis demonstrated that this bundling activity resembled that of α-actinin. Biochemical experiments revealed that bundling was not achieved by myopodin's ability to dimerize, indicating the presence of two individual F-actin binding sites within the second binding segment. Thus full length myopodin contains at least three F-actin binding sites. These data provide further understanding of the mechanisms by which myopodin contributes to actin reorganization during myofibril assembly.
机译：横纹肌肌原纤维的组装是一个多步骤过程，其中涉及多种蛋白质。肌纤维形成的第一步和最重要的步骤之一是将薄的肌丝排列成有序的I-Z-I刷，这需要许多肌动蛋白结合蛋白的协同活性。肌节蛋白在肌节α-肌动蛋白之前的早期表达及其与肌动蛋白，α-肌动蛋白和丝质蛋白的结合，表明该蛋白在肌动蛋白细胞骨架重塑中起着重要作用，而肌蛋白在此过程中的确切功能尚待解决。 。虽然以前将肌足蛋白描述为能够在短暂转染时将肌动蛋白丝交联成粗束的蛋白质，但尚不清楚单独的肌足蛋白是否能够使肌动蛋白束缚，或者是否涉及其他蛋白。因此，我们研究了肌球蛋白的体外肌动蛋白结合特性。用骨骼肌肌动蛋白进行的高速共沉淀试验证实了肌足蛋白与F-肌动蛋白的直接结合，并表明这种相互作用是由至少两个独立的肌动蛋白结合位点介导的，这在迄今为止确定的所有肌足蛋白同工型中都存在。此外，低速沉降分析法表明，不仅全长的肌足蛋白，而且仅包含第二个结合位点的片段在不存在辅助蛋白的情况下也会束缚微丝。超微结构分析表明，这种结合活性类似于α-肌动蛋白。生化实验表明，肌球蛋白的二聚能力不能实现捆绑作用，这表明第二个结合区内存在两个单独的F-肌动蛋白结合位点。因此，全长肌足蛋白含有至少三个F-肌动蛋白结合位点。这些数据提供了对肌足蛋白在肌原纤维组装过程中有助于肌动蛋白重组的机制的进一步理解。

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