Drebrin attenuates the interaction between actin and myosin-V

• Published in: Biochemical and biophysical research communications Vol. 359; no. 2; pp. 398 - 401
• Main Authors: Ishikawa, Ryoki, Katoh, Kaoru, Takahashi, Ayumi, Xie, Ce, Oseki, Koushi, Watanabe, Michitoshi, Igarashi, Michihiro, Nakamura, Akio, Kohama, Kazuhiro
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 27.07.2007
• Subjects: Actin dynamics; Actin-binding protein; Actins - metabolism; Adenosine Triphosphatases - metabolism; Animals; ATPase; Ca(2+) Mg(2+)-ATPase - chemistry; Dendrites - metabolism; Dendritic Cells - metabolism; Dendritic spine; DNA, Complementary - metabolism; Dose-Response Relationship, Drug; Drebrin; In vitro motility assay; Myosin Type V - metabolism; Myosin-V; Myosins - chemistry; Neurons - metabolism; Neuropeptides - biosynthesis; Neuropeptides - chemistry; Protein Binding; Rats; Drebrin; Myosin-V; In vitro motility assay; Actin dynamics; ATPase; Dendritic spine; Actin-binding protein
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2007.05.123

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.