title: Interplay of enzymatic and structural functions of CaMKII in long-term potentiation.
abstract: Since the discovery of long-term potentiation (LTP) about a half-century ago, Ca2+/CaM-dependent protein kinase II (CaMKII) has been one of the most extensively studied components of the molecular machinery that regulate plasticity. This unique dodecameric kinase complex plays pivotal roles in LTP by phosphorylating substrates through elaborate regulatory mechanisms, and is known to be both necessary and sufficient for LTP. In addition to acting as a kinase, CaMKII has been postulated to have structural roles because of its extraordinary abundance and diverse interacting partners. It now is becoming clear that these two functions of CaMKII cooperate closely for the induction of both functional and structural synaptic plasticity of dendritic spines. Because of its extraordinary abundance within neuronal cells, calmodulin kinase CaMKII has been believed to act as a structural protein as well as an enzyme during synaptic plasticity. In this review, we summarized studies in CaMKII field and provide an insight into how enzymatic and structural functions of CaMKII cooperate with each other for long-term potentiation (LTP) in neurons. This article is part of a mini review series: "Synaptic Function and Dysfunction in Brain Diseases".
authors.affiliation: Brain Science Institute, RIKEN, Wako, Saitama, Japan.
authors.forename: Karam
authors.initials: K
authors.lastname: Kim
authors.affiliation: Brain Science Institute, RIKEN, Wako, Saitama, Japan.
authors.forename: Takeo
authors.initials: T
authors.lastname: Saneyoshi
authors.affiliation: Brain Science Institute, RIKEN, Wako, Saitama, Japan.
authors.forename: Tomohisa
authors.initials: T
authors.lastname: Hosokawa
authors.affiliation: Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada.|Department of Molecular Genetics, Faculty of Medicine, University of Toronto, Toronto, ON, Canada.
authors.forename: Kenichi
authors.initials: K
authors.lastname: Okamoto
authors.affiliation: Brain Science Institute, RIKEN, Wako, Saitama, Japan.|Saitama University Brain Science Institute, Saitama University, Saitama, Japan.|School of Life Science, South China Normal University, Guangzhou, China.
authors.forename: Yasunori
authors.initials: Y
authors.lastname: Hayashi
mesh_terms: D000818:Animals; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2 / Q000737:chemistry* / Q000378:metabolism*; D049229:Dendritic Spines / Q000201:enzymology; D006624:Hippocampus / Q000201:enzymology*; D006801:Humans; D017774:Long-Term Potentiation / Q000502:physiology*; D008870:Microtubules / Q000201:enzymology; D009473:Neuronal Plasticity / Q000502:physiology
chemical_list: D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2
keywords: CaMKII; cytoskeleton; synaptic plasticity