TY - JOUR
T1 - Drebrin attenuates the interaction between actin and myosin-V
AU - Ishikawa, Ryoki
AU - Katoh, Kaoru
AU - Takahashi, Ayumi
AU - Xie, Ce
AU - Oseki, Koushi
AU - Watanabe, Michitoshi
AU - Igarashi, Michihiro
AU - Nakamura, Akio
AU - Kohama, Kazuhiro
N1 - Funding Information:
We thank Dr. Tomoaki Shirao (Gunma University, Japan) for supplying cDNA for rat drebrin-A. This work was supported by a Grant-in-Aid for Scientific Research on Priority Areas—Regulation of Nano-Systems in Cells—from the Ministry of Education, Science, and Culture of Japan (to R.I.).
PY - 2007/7/27
Y1 - 2007/7/27
N2 - 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.
AB - 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.
KW - Actin dynamics
KW - Actin-binding protein
KW - ATPase
KW - Dendritic spine
KW - Drebrin
KW - In vitro motility assay
KW - Myosin-V
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U2 - 10.1016/j.bbrc.2007.05.123
DO - 10.1016/j.bbrc.2007.05.123
M3 - Article
C2 - 17543276
AN - SCOPUS:34249948905
SN - 0006-291X
VL - 359
SP - 398
EP - 401
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -