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

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)398-401
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2007 Jul 27


  • Actin dynamics
  • Actin-binding protein
  • ATPase
  • Dendritic spine
  • Drebrin
  • In vitro motility assay
  • Myosin-V


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