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首页> 外文期刊>Journal of Molecular Biology >Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments
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Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments

机译：Metavinculin调整了Vinculin诱导的肌动蛋白丝束的柔性和结构

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Vinculin is an abundant protein found at cell-cell and cell-extracellular matrix junctions. In muscles, a longer splice isoform of vinculin, metavinculin, is also expressed. The metavinculin-specific insert is part of the C-terminal tail domain, the actin-binding site of both isoforms. Mutations in the metavinculin-specific insert are linked to heart disease such as dilated cardiomyopathies. Vinculin tail domain (VT) both binds and bundles actin filaments. Metavinculin tail domain (MVT) binds actin filaments in a similar orientation but does not bundle filaments. Recently, MVT was reported to sever actin filaments. In this work, we asked how MVT influences F-actin alone or in combination with VT. Cosedimentation and limited proteolysis experiments indicated a similar actin binding affinity and mode for both VT and MVT. In real-time total internal reflection fluorescence microscopy experiments, MVT's severing activity was negligible. Instead, we found that MVT binding caused a 2-fold reduction in F-actin's bending persistence length and increased susceptibility to breakage. Using mutagenesis and site-directed labeling with fluorescence probes, we determined that MVT alters actin interprotomer contacts and dynamics, which presumably reflect the observed changes in bending persistence length. Finally, we found that MVT decreases the density and thickness of actin filament bundles generated by VT. Altogether, our data suggest that MVT alters actin filament flexibility and tunes filament organization in the presence of VT. Both of these activities are potentially important for muscle cell function. Perhaps MVT allows the load of muscle contraction to act as a signal to reorganize actin filaments. (C) 2015 Elsevier Ltd. All rights reserved.
机译：Vinculin是一种在细胞-细胞和细胞-细胞外基质连接处发现的丰富蛋白质。在肌肉中，还表达了较长的纽蛋白，metavinculin剪接异构体。 metavinculin特异的插入片段是C末端尾部结构域的一部分，C尾部结构域是两种同工型的肌动蛋白结合位点。 metavinculin特异性插入片段中的突变与心脏病（如扩张型心肌病）有关。 Vinculin尾结构域（VT）既绑定并捆绑肌动蛋白丝。 Metavinculin尾结构域（MVT）以相似的方向结合肌动蛋白丝，但不捆束丝。最近，据报道MVT切断肌动蛋白丝。在这项工作中，我们询问了MVT如何单独或与VT一起影响F-肌动蛋白。沉淀和有限的蛋白水解实验表明，VT和MVT的肌动蛋白结合亲和力和模式相似。在实时全内反射荧光显微镜实验中，MVT的切断活性可忽略不计。相反，我们发现MVT结合会导致F-肌动蛋白的弯曲持久性长度减少2倍，并增加了断裂的敏感性。使用诱变和荧光探针的定点标记，我们确定MVT改变肌动蛋白间质接触和动力学，这大概反映了观察到的弯曲持久性长度的变化。最后，我们发现MVT降低了VT产生的肌动蛋白丝束的密度和厚度。总而言之，我们的数据表明MVT在存在VT的情况下会改变肌动蛋白丝的柔韧性并调节丝的组织。这两种活动对于肌肉细胞功能都可能很重要。也许MVT允许肌肉收缩负荷充当重组肌动蛋白丝的信号。 （C）2015 Elsevier Ltd.保留所有权利。

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