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

ABSTRACT: 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. Increasingly, computational models are used to explore synaptic plasticity and the mechanisms regulating CaMKII activity. Conventional modeling approaches may exclude biophysical detail due to the impractical number of state combinations that arise when explicitly monitoring the conformational changes, ligand binding, and phosphorylation events that occur on each of the CaMKII holoenzyme's subunits. To manage the combinatorial explosion without necessitating bias or loss in biological accuracy, we use a

SUBMITTER: Pharris MC 

PROVIDER: S-EPMC6957207 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature