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肌动蛋白动力学的随机模拟揭示了退火和断裂的作用。

Stochastic simulation of actin dynamics reveals the role of annealing and fragmentation.

作者信息

Fass Joseph, Pak Chi, Bamburg James, Mogilner Alex

机构信息

Department of Neurobiology, Physiology and Behavior, University of California, Davis, CA 95616-8633, USA.

出版信息

J Theor Biol. 2008 May 7;252(1):173-83. doi: 10.1016/j.jtbi.2008.01.001. Epub 2008 Jan 11.

Abstract

Recent observations of F-actin dynamics call for theoretical models to interpret and understand the quantitative data. A number of existing models rely on simplifications and do not take into account F-actin fragmentation and annealing. We use Gillespie's algorithm for stochastic simulations of the F-actin dynamics including fragmentation and annealing. The simulations vividly illustrate that fragmentation and annealing have little influence on the shape of the polymerization curve and on nucleotide profiles within filaments but drastically affect the F-actin length distribution, making it exponential. We find that recent surprising measurements of high length diffusivity at the critical concentration cannot be explained by fragmentation and annealing events unless both fragmentation rates and frequency of undetected fragmentation and annealing events are greater than previously thought. The simulations compare well with experimentally measured actin polymerization data and lend additional support to a number of existing theoretical models.

摘要

最近对F-肌动蛋白动力学的观察需要理论模型来解释和理解定量数据。许多现有模型依赖于简化,没有考虑F-肌动蛋白的断裂和退火。我们使用 Gillespie算法对包括断裂和退火在内的F-肌动蛋白动力学进行随机模拟。模拟结果生动地表明,断裂和退火对聚合曲线的形状和细丝内的核苷酸谱影响很小,但对F-肌动蛋白长度分布有显著影响,使其呈指数分布。我们发现,除非断裂速率以及未检测到的断裂和退火事件的频率大于先前的设想,否则最近在临界浓度下对高长度扩散率的惊人测量结果无法用断裂和退火事件来解释。模拟结果与实验测量的肌动蛋白聚合数据比较吻合,并为许多现有理论模型提供了额外支持。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cffe/2386518/dcf9cf9143d9/nihms49398f1.jpg

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