Drebrin attenuates the interaction between actin and myosin-V

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) 3918–3...

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Published in:Biochemical and biophysical research communications 2007-07, Vol.359 (2), p.398-401
Main Authors: Ishikawa, Ryoki, Katoh, Kaoru, Takahashi, Ayumi, Xie, Ce, Oseki, Koushi, Watanabe, Michitoshi, Igarashi, Michihiro, Nakamura, Akio, Kohama, Kazuhiro
Format: Article
Language:English
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
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.05.123