A multi-state model of the CaMKII dodecamer suggests a role for calmodulin in maintenance of autophosphorylation

Ca2+/calmodulin-dependent protein kinase II (CaMKII) accounts for up to 2 percent of all brain protein and is essential to memory function. CaMKII activity is known to regulate dynamic shifts in the size and signaling strength of neuronal connections, a process known as synaptic plasticity. Increasi...

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Veröffentlicht in:	PLoS computational biology 2019-12, Vol.15 (12), p.e1006941-e1006941
Hauptverfasser:	Pharris, Matthew C, Patel, Neal M, VanDyk, Tyler G, Bartol, Thomas M, Sejnowski, Terrence J, Kennedy, Mary B, Stefan, Melanie I, Kinzer-Ursem, Tamara L
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Binding Sites Biology and Life Sciences Biomedical engineering Biophysical Phenomena Ca2+/calmodulin-dependent protein kinase II Calcium - metabolism Calcium ions Calcium-binding protein Calcium-Calmodulin-Dependent Protein Kinase Type 2 - chemistry Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism Calmodulin Calmodulin - metabolism Combinatorial analysis Computational Biology Computational neuroscience Crystal structure Engineering Enzyme Stability Explosions Funding Hippocampus - metabolism Humans Kinases Maintenance Methods Models, Molecular Models, Neurological Molecular modelling Neuronal Plasticity Phosphatase Phosphoprotein Phosphatases - metabolism Phosphorylation Plasticity Protein Binding Protein phosphatase Protein Structure, Quaternary Protein Subunits Proteins Research and Analysis Methods Software Supervision Synaptic plasticity
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