CaMKII and the actin-crosslinking protein α-actinin-2 associate within minutes of the induction of long-term potentiation and disrupting this interaction prevents formation of enlarged dendritic spines.

Longevity in C. elegans is influenced not only by insulin/IGF-1 signalling, but also by CAMKII and calcineurin, acting on the same target, the transcription factor DAF-16.

Activation of CaMKII holoenzymes triggers the exchange of subunits with other holoenzymes, including unactivated ones, enabling the calcium-independent phosphorylation and activation of new subunits.

A biallelic missense mutation in the highly conserved, neuron-specific kinase CAMK2A abrogates holoenzyme assembly and causes a new inherited neurodevelopmental disease.

Physiology studies demonstrate that CaMKII is a molecular storage device.

Differences in the flexible linkers connecting the kinase domain to an oligomeric hub modulate CaMKII activity by changing the balance between activating and inhibitory autophosphorylation.

Due to subunit-exchange, CaMKII can store information at diverse time-scales and might play a central role in the memory maintenance.

Activation and autophosphorylation of CaMKII releases the regulatory segment, which can then bind to and destabilize the hub assembly by trapping large fluctuations in the hub architecture.

Optogenetically activated individual descending neurons in Drosophila melanogaster drive varied stereotyped motor patterns that are often influenced by the animal's initial behavioral state.

CaMKII is capable of spreading activity between holoenzymes without exchanging subunits.