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Drebrin attenuates the interaction between actin and myosin-V.

Authors: Ishikawa, R  Katoh, K  Takahashi, A  Xie, C  Oseki, K  Watanabe, M  Igarashi, M  Nakamura, A  Kohama, K 
Citation: Ishikawa R, etal., Biochem Biophys Res Commun. 2007 Jul 27;359(2):398-401. Epub 2007 May 25.
Pubmed: (View Article at PubMed) PMID:17543276
DOI: Full-text: 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.

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CRRD Object Information
CRRD ID: 10398727
Created: 2015-09-08
Species: All species
Last Modified: 2015-09-08
Status: ACTIVE



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