title: Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex.
abstract: Morphological changes in the dendritic spines have been postulated to participate in the expression of synaptic plasticity. The cytoskeleton is likely to play a key role in regulating spine structure. Here we examine the molecular mechanisms responsible for the changes in spine morphology, focusing on drebrin, an actin-binding protein that is known to change the properties of actin filaments. We found that adult-type drebrin is localized in the dendritic spines of rat forebrain neurons, where it binds to the cytoskeleton. To identify the cytoskeletal proteins that associated with drebrin, we isolated drebrin-containing cytoskeletons using immunoprecipitation with a drebrin antibody. Drebrin, actin, myosin, and gelsolin were co-precipitated. We next examined the effect of drebrin on actomyosin interaction. In vitro, drebrin reduced the sliding velocity of actin filaments on immobilized myosin and inhibited the actin-activated ATPase activity of myosin. These results suggest that drebrin may modulate the actomyosin interaction within spines and may play a role in the structure-based plasticity of synapses.
authors.affiliation: Department of Neurobiology and Behavior, Gunma University School of Medicine, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Hayashi
authors.forename: R
authors.initials: R
authors.lastname: Ishikawa
authors.forename: L H
authors.initials: LH
authors.lastname: Ye
authors.forename: X L
authors.initials: XL
authors.lastname: He
authors.forename: K
authors.initials: K
authors.lastname: Takata
authors.forename: K
authors.initials: K
authors.lastname: Kohama
authors.forename: T
authors.initials: T
authors.lastname: Shirao
mesh_terms: D000199:Actins / Q000032:analysis / Q000378:metabolism; D000205:Actomyosin / Q000037:antagonists & inhibitors; D000367:Age Factors; D000818:Animals; D001923:Brain Chemistry; D002540:Cerebral Cortex / Q000166:cytology*; D003599:Cytoskeleton / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism; D003712:Dendrites / Q000737:chemistry / Q000648:ultrastructure*; D018260:Gelsolin / Q000032:analysis / Q000378:metabolism; D015151:Immunoblotting; D007536:Isomerism; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D009218:Myosins / Q000032:analysis / Q000378:metabolism; D009474:Neurons / Q000737:chemistry / Q000648:ultrastructure; D009479:Neuropeptides / Q000032:analysis / Q000737:chemistry / Q000502:physiology*; D016548:Prosencephalon / Q000737:chemistry; D011485:Protein Binding / Q000502:physiology; D051381:Rats; D017208:Rats, Wistar; D013569:Synapses / Q000737:chemistry; D013570:Synaptic Membranes / Q000737:chemistry; D013574:Synaptosomes / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D000199:Actins; D018260:Gelsolin; D009479:Neuropeptides; C053386:drebrins; D000205:Actomyosin; D009218:Myosins