Lieleg O, Schmoller K M, Claessens M M A E, Bausch A R
Lehrstuhl für Zellbiophysik E27, Technische Universität München, Garching, Germany.
Biophys J. 2009 Jun 3;96(11):4725-32. doi: 10.1016/j.bpj.2009.03.038.
Although the structure of cross-linking molecules mainly determines the structural organization of actin filaments and with that the static elastic properties of the cytoskeleton, it is largely unknown how the biochemical characteristics of transiently cross-linking proteins (actin-binding proteins (ABPs)) affect the viscoelasticity of actin networks. In this study, we show that the macroscopic network response of reconstituted actin networks can be traced back to the microscopic interaction potential of an individual actin/ABP bond. The viscoelastic response of cross-linked actin networks is set by the cross-linker off-rate, the binding energy, and the characteristic bond length of individual actin/ABP interactions.
尽管交联分子的结构主要决定了肌动蛋白丝的结构组织,进而决定了细胞骨架的静态弹性特性,但目前很大程度上尚不清楚瞬时交联蛋白(肌动蛋白结合蛋白,ABP)的生化特性如何影响肌动蛋白网络的粘弹性。在本研究中,我们表明,重构肌动蛋白网络的宏观网络响应可追溯到单个肌动蛋白/ABP键的微观相互作用势。交联肌动蛋白网络的粘弹性响应由交联剂解离速率、结合能以及单个肌动蛋白/ABP相互作用的特征键长决定。