Drebrin attenuates the interaction between actin and myosin-V
Drebrin attenuates the interaction between actin and myosin-V
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DOI：
10.1016/j.bbrc.2007.05.123
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发表时间：
2007-07-27
影响因子：
3.1
通讯作者：
Kohama, Kazuhiro
中科院分区：
文献类型：
--
作者：
Ishikawa, Ryoki;Katoh, Kaoru;Kohama, Kazuhiro
Drebrin-A 是一种肌动蛋白结合蛋白，位于成熟神经元的树突棘中，并且被认为会影响树突棘的形态 [K. Hayashi，T. Shirao，培养的皮层神经元中 Drebrin 过度表达引起的树突棘形状变化，J. Neurosci。 19（1999）3918-3925]。然而，尚未报道drebrin-A的生化分析。在这项研究中，我们使用细菌表达系统纯化了drebrin-A，并在体外对其进行了表征。 Drebrin-A 与肌动蛋白丝结合，化学计量为 1 个 Drebrin 分子与 5-6 个肌动蛋白分子。此外，drebrin-A 降低了肌球蛋白 V 的 Mg-ATPase 活性。在硝基运动测定中，结果显示，drebrin-A 减少了 F-actin 与肌球蛋白-V 包被的玻璃表面的附着，但一旦 F-actin 附着到表面，F-actin 的滑动速度就不受 drebrin A 的存在影响。这些发现表明，drebrin-A 可能会影响脊柱动力学、囊泡运输和其他功能。肌球蛋白-V 通过减弱肌动蛋白和肌球蛋白-V 之间的相互作用来驱动神经元的运动。 (c) 2007 Elsevier Inc. 保留所有权利。
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 nitro 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. (c) 2007 Elsevier Inc. All rights reserved.