协同效应范围对肌动蛋白结合蛋白簇大小、密度和动力学的影响
The Range of Cooperativity Modulates Actin Binding Protein Cluster Size, Density and Dynamics
摘要：
肌动蛋白细胞骨架由多个网络组成，这些网络专门用于几个过程，如细胞运动或细胞分裂。这些网络中的每一个都由有组织的肌动蛋白微丝组成，这些微丝被特定的肌动蛋白结合蛋白（ABP）修饰。引导ABP到特定肌动蛋白网络的分子机制仍然知之甚少，但协同性，ABP的结合受到近端结合的ABP的积极影响的机制，在产生局部密集的ABP延伸中起着至关重要的作用。协同结合的特征在于其幅度，但也通过其效应通过长程变构相互作用沿肌动蛋白丝传播的范围。这些变构效应的范围仍有争议，但可能是显着的肌动蛋白丝在细胞中的长度尺度。在这里，我们研究了协同性如何影响ABPs的聚类，使用ABPs与肌动蛋白丝结合的随机计算模型。该模型再现了实验观察到的形成ABP集群在单丝规模，并提供了一个理论估计的范围内的协同蛋白质，如ADF/cofilin。我们发现，幅度和空间范围的协同性显着影响聚类的属性。然而，协同性的参数调制不同的组装速率，大小和动态的ABP集群，这表明协同性是一种有效的机制，以精确地调节招聘的ABP在细胞中。这项工作提供了一个更一般的框架，为未来的理解如何肌动蛋白网络获得不同的和特定的蛋白质组合物从一个共同的细胞质。
英文摘要：
The actin cytoskeleton is composed of multiple networks which are specialized for several processes such as cell motility or cell division. Each of these networks are composed of organized actin microfilaments which are decorated with specific sets of actin binding proteins (ABPs). The molecular mechanisms guiding ABPs to specific actin networks are still poorly understood, but cooperativity, the mechanism by which the binding of an ABP is positively influenced by proximal bound ABPs, plays a crucial role in generating locally dense stretches of ABPs. Cooperative binding is characterized by its amplitude, but also by the range at which its effects are propagated along an actin filament through long-range allosteric interactions. The range of these allosteric effects is still debated, but is likely to be significant at the lengthscale of actin filaments in cells. Here, we investigated how cooperativity influences the clustering of ABPs, using a stochastic computational model of binding of ABPs to actin filaments. The model reproduces the formation of ABP clusters observed experimentally at the single filament scale, and provides a theoretical estimation of the range of cooperativity for proteins such as ADF/cofilin. We found that both the amplitude and the spatial range of cooperativity dramatically impact the properties of clustering. However, the parameters of cooperativity modulate differently the rate of assembly, size and dynamics of the ABP clusters, suggesting that cooperativity is an efficient mechanism to regulate precisely the recruitment of ABPs in cells. This work provides a more general framework for future understanding of how actin networks acquire distinct and specific protein compositions from a common cytoplasm.
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