Kuhlman Philip A
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, UK.
Cell Motil Cytoskeleton. 2005 May;61(1):1-8. doi: 10.1002/cm.20061.
During actin polymerization, it has been theorized that the actin filament length distribution initially grows in the form of a Gaussian before converting to produce that of an exponential. However, it has been difficult to demonstrate this experimentally. In this study, we use modern fluorescence microscopy techniques to observe the changing actin filament length distribution during and subsequent to the polymerization process. Nucleated actin filament growth using barbed end capping proteins (gelsolin and erythrocyte capping protein) leads to Gaussian length distributions that are relatively stable. As predicted, nucleated actin filament growth using actin/spectrin complexes follows a similar process until polymerization reaches equilibrium whereafter the Gaussian length distribution rapidly converts to that of an exponential. This study provides direct confirmation of the original theories for the mode of actin polymerization but raises doubts regarding the mechanism of the length distribution conversion from Gaussian to exponential.
在肌动蛋白聚合过程中,理论上认为肌动蛋白丝长度分布最初以高斯分布的形式增长,然后转变为指数分布。然而,很难通过实验证明这一点。在本研究中,我们使用现代荧光显微镜技术观察聚合过程中及之后肌动蛋白丝长度分布的变化。使用带刺末端封端蛋白(凝溶胶蛋白和红细胞封端蛋白)的成核肌动蛋白丝生长会导致相对稳定的高斯长度分布。正如预测的那样,使用肌动蛋白/血影蛋白复合物的成核肌动蛋白丝生长遵循类似的过程,直到聚合达到平衡,此后高斯长度分布迅速转变为指数分布。这项研究直接证实了肌动蛋白聚合模式的原始理论,但对长度分布从高斯分布转变为指数分布的机制提出了疑问。