Drebrin attenuates the interaction between actin and myosin-V

Ryoki Ishikawa, Kaoru Katoh, Ayumi Takahashi, Ce Xie, Koushi Oseki, Michitoshi Watanabe, Michihiro Igarashi, Akio Nakamura, Kazuhiro Kohama

研究成果: Article査読

33 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)398-401
ページ数4
ジャーナルBiochemical and biophysical research communications
359
2
DOI
出版ステータスPublished - 2007 7月 27
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

フィンガープリント

「Drebrin attenuates the interaction between actin and myosin-V」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル