Overview:

Ca2+/calmodulin-dependent protein kinase II (CAMK2) is a multi-functional calcium and calmodulin-dependent serine/threonine kinase that mediates cellular responses to a wide variety of intercellular signals (1). CAMK2 is abundant in the brain and has been shown to regulate diverse cellular functions including synaptic plasticity, neurotransmitter synthesis and release, gene expression, ion channel function, carbohydrate metabolism, cytoskeletal function, and Ca2+-homeostasis (2,3). Phosphorylation of Thr286 produces an autonomously active form of CAMK2 (4). Autophosphorylation of Thr305 inhibits the activity CAMK2, which leads to reduced localization to the postsynaptic density and consequently reduced neuronal plasticity and capacity for learning (5).

References:

1. Kennedy, M B.: Signal transduction molecules at the glutamatergic postsynaptic membrane. 1998 Brain Res Rev 1998 26:243-257.

2. Gleason, M R. et al: Translocation of CaM kinase II to synaptic sites in vivo. Nature Neurosci 2003 6:217-218.

3. Hudmon, A. et al: Neuronal Ca2+/calmodulin-dependent protein kinase II: The role of structure and autoregulation in cellular function. Annu Rev Biochem 2002 71:473-510.

4. Meng, F J. et al: Autophosphorylated calcium/calmodulin-dependent protein kinase IIa (CaMKIIa) reversibly targets to and phosphorylates N-methyl-D-aspartate receptor subunit 2B (NR2B) in cerebral ischemia and reperfusion in hippocampus of rats. Brain Res 2003 967:161-169.

5. Elgersma, Y. et al: Inhibitory autophosphorylation of CaMKII controls PSD association, plasticity, and learning. Neuron 200236:493-505.