title: Cadherin activity is required for activity-induced spine remodeling.
abstract: Neural activity induces the remodeling of pre- and postsynaptic membranes, which maintain their apposition through cell adhesion molecules. Among them, N-cadherin is redistributed, undergoes activity-dependent conformational changes, and is required for synaptic plasticity. Here, we show that depolarization induces the enlargement of the width of spine head, and that cadherin activity is essential for this synaptic rearrangement. Dendritic spines visualized with green fluorescent protein in hippocampal neurons showed an expansion by the activation of AMPA receptor, so that the synaptic apposition zone may be expanded. N-cadherin-venus fusion protein laterally dispersed along the expanding spine head. Overexpression of dominant-negative forms of N-cadherin resulted in the abrogation of the spine expansion. Inhibition of actin polymerization with cytochalasin D abolished the spine expansion. Together, our data suggest that cadherin-based adhesion machinery coupled with the actin-cytoskeleton is critical for the remodeling of synaptic apposition zone.
authors.affiliation: Department of Pharmacology, Osaka University Medical School, Suita, Japan.
authors.forename: Ko
authors.initials: K
authors.lastname: Okamura
authors.forename: Hidekazu
authors.initials: H
authors.lastname: Tanaka
authors.forename: Yoshiki
authors.initials: Y
authors.lastname: Yagita
authors.forename: Yoshinaga
authors.initials: Y
authors.lastname: Saeki
authors.forename: Akihiko
authors.initials: A
authors.lastname: Taguchi
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Hiraoka
authors.forename: Ling-Hui
authors.initials: LH
authors.lastname: Zeng
authors.forename: David R
authors.initials: DR
authors.lastname: Colman
authors.forename: Naomasa
authors.initials: N
authors.lastname: Miki
mesh_terms: D000199:Actins / Q000037:antagonists & inhibitors / Q000096:biosynthesis; D000200:Action Potentials / Q000502:physiology; D000818:Animals; D015820:Cadherins / Q000235:genetics / Q000378:metabolism*; D002478:Cells, Cultured; D015638:Cytochalasin D / Q000494:pharmacology; D049229:Dendritic Spines / Q000378:metabolism* / Q000648:ultrastructure; D019706:Excitatory Postsynaptic Potentials / Q000502:physiology; D049452:Green Fluorescent Proteins / Q000378:metabolism; D006624:Hippocampus / Q000166:cytology / Q000378:metabolism*; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009473:Neuronal Plasticity / Q000502:physiology*; D051381:Rats; D018091:Receptors, AMPA / Q000378:metabolism; D011993:Recombinant Fusion Proteins; D013570:Synaptic Membranes / Q000378:metabolism; D009435:Synaptic Transmission / Q000502:physiology*
chemical_list: D000199:Actins; D015820:Cadherins; D009419:Nerve Tissue Proteins; D018091:Receptors, AMPA; D011993:Recombinant Fusion Proteins; C033652:postsynaptic density proteins; D049452:Green Fluorescent Proteins; D015638:Cytochalasin D