drebrin减弱肌动蛋白和肌球蛋白-V之间的相互作用。
Drebrin attenuates the interaction between actin and myosin-V.
作者信息
Ishikawa Ryoki, Katoh Kaoru, Takahashi Ayumi, Xie Ce, Oseki Koushi, Watanabe Michitoshi, Igarashi Michihiro, Nakamura Akio, Kohama Kazuhiro
机构信息
Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, Maebashi, Gunma, Japan.
出版信息
Biochem Biophys Res Commun. 2007 Jul 27;359(2):398-401. doi: 10.1016/j.bbrc.2007.05.123. Epub 2007 May 25.
Drebrin-A is an actin-binding protein localized in the dendritic spines of mature neurons, and has been suggested to affect spine morphology [K. Hayashi, T. Shirao, Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons, J. Neurosci. 19 (1999) 3918-3925]. However, no biochemical analysis of drebrin-A has yet been reported. In this study, we purified drebrin-A using a bacterial expression system, and characterized it in vitro. Drebrin-A bound to actin filaments with a stoichiometry of one drebrin molecule to 5-6 actin molecules. Furthermore, drebrin-A decreased the Mg-ATPase activity of myosin V. In vitro motility assay revealed that the attachment of F-actin to glass surface coated with myosin-V was decreased by drebrin-A, but once F-actin attached to the surface, the sliding speed of F-actin was unaffected by the presence of drebrin A. These findings suggest that drebrin-A may affect spine dynamics, vesicle transport, and other myosin-V-driven motility in neurons through attenuating the interaction between actin and myosin-V.
双调蛋白-A是一种肌动蛋白结合蛋白，定位于成熟神经元的树突棘中，有人认为它会影响棘的形态[K. 林、T. 白尾，培养的皮质神经元中双调蛋白过表达导致树突棘形状的改变，《神经科学杂志》19 (1999) 3918 - 3925]。然而，尚未有关于双调蛋白-A的生化分析报道。在本研究中，我们使用细菌表达系统纯化了双调蛋白-A，并对其进行了体外特性鉴定。双调蛋白-A以一个双调蛋白分子与5 - 6个肌动蛋白分子的化学计量比与肌动蛋白丝结合。此外，双调蛋白-A降低了肌球蛋白V的Mg-ATP酶活性。体外运动分析表明，双调蛋白-A降低了F-肌动蛋白与涂有肌球蛋白-V的玻璃表面的附着，但一旦F-肌动蛋白附着在表面，F-肌动蛋白的滑动速度不受双调蛋白A存在的影响。这些发现表明，双调蛋白-A可能通过减弱肌动蛋白与肌球蛋白-V之间的相互作用来影响神经元中的棘动态、囊泡运输以及其他由肌球蛋白-V驱动的运动。
Zotero 插件