Honda M, Takiguchi K, Ishikawa S, Hotani H
Department of Molecular Biology, Graduate School of Science, Nagoya University, Furo-cho, Nagoya, Chikusa-ku, 464-8602, Japan.
J Mol Biol. 1999 Mar 26;287(2):293-300. doi: 10.1006/jmbi.1999.2592.
To study the morphogenesis of cells caused by the organization of their internal cytoskeletal network, we characterized the transformation of liposomes encapsulating actin and its crosslinking proteins, fascin, alpha-actinin, or filamin, using real-time high-intensity dark-field microscopy. With increasing temperature, the encapsulated G-actin polymerized into actin filaments and formed bundles or gels, depending on the type of actin-crosslinking protein that was co-encapsulated, causing various morphological changes of liposomes. The differences in morphology among transformed liposomes indicate that actin-crosslinking proteins determine liposome shape by organizing their specific actin networks. Morphological analysis reveals that the crosslinking manner, i.e. distance and angular flexibility between adjacent crosslinked actin filaments, is essential for the morphogenesis rather than their binding affinity and stoichiometry to actin filaments.
为了研究细胞内部细胞骨架网络的组织所引起的细胞形态发生，我们使用实时高强度暗场显微镜对包裹肌动蛋白及其交联蛋白（成束蛋白、α-辅肌动蛋白或细丝蛋白）的脂质体的转变进行了表征。随着温度升高，包裹的G-肌动蛋白聚合成肌动蛋白丝，并根据共包裹的肌动蛋白交联蛋白的类型形成束状或凝胶状，从而导致脂质体发生各种形态变化。转化后的脂质体在形态上的差异表明，肌动蛋白交联蛋白通过组织其特定的肌动蛋白网络来决定脂质体的形状。形态学分析表明，交联方式，即相邻交联肌动蛋白丝之间的距离和角度灵活性，对形态发生至关重要，而不是它们与肌动蛋白丝的结合亲和力和化学计量比。
