Yuta Ishizuka    Department   Kawasaki Medical School  Kawasaki Medical School, Department of Pathophysiology and Metabolism,    Position   Assistant Professor
Article types	原著
Language	English
Peer review	Peer reviewed
Title	Myosin II ATPase activity mediates the long-term potentiation-induced exodus of stable F-actin bound by drebrin A from dendritic spines.
Journal	Formal name：PloS one Abbreviation：PLoS One ISSN code：19326203/19326203
Domestic / Foregin	Foregin
Publisher	PLOS
Volume, Issue, Page	9(1),pp.e85367
Author and coauthor	Toshiyuki Mizui, Yuko Sekino, Hiroyuki Yamazaki, Yuta Ishizuka, Hideto Takahashi, Nobuhiko Kojima, Masami Kojima , Tomoaki Shirao
Publication date	2014/01
Summary	The neuronal actin-binding protein drebrin A forms a stable structure with F-actin in dendritic spines. NMDA receptor activation causes an exodus of F-actin bound by drebrin A (DA-actin) from dendritic spines, suggesting a pivotal role for DA-actin exodus in synaptic plasticity. We quantitatively assessed the extent of DA-actin localization to spines using the spine-dendrite ratio of drebrin A in cultured hippocampal neurons, and found that (1) chemical long-term potentiation (LTP) stimulation induces rapid DA-actin exodus and subsequent DA-actin re-entry in dendritic spines, (2) Ca(2+) influx through NMDA receptors regulates the exodus and the basal accumulation of DA-actin, and (3) the DA-actin exodus is blocked by myosin II ATPase inhibitor, but is not blocked by myosin light chain kinase (MLCK) or Rho-associated kinase (ROCK) inhibitors. These results indicate that myosin II mediates the interaction between NMDA receptor activation and DA-actin exodus in LTP induction. Furthermore, myosin II seems to be activated by a rapid actin-linked mechanism rather than slow MLC phosphorylation. Thus the myosin-II mediated DA-actin exodus might be an initial event in LTP induction, triggering actin polymerization and spine enlargement.
DOI	10.1371/journal.pone.0085367
PMID	24465547