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.

The α1 isoform of synGAP restricts the binding of AMPA-receptors and other regulatory proteins to PSD-95, and thus regulates synaptic strength.

Closed-ring and open-spiral assembly of the multi-subunit neuronal kinase CaMKII suggest a mechanism for how active subunits shuttle between individual assemblies, propagating stimulatory signals.

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.

With the new Ankyrin-G-GFP reporter line, researchers can visualize and study neuronal compartments critical for signal transduction without affecting neuronal activity and subcellular integrity of the cells under investigation.

Detailed SYNGAP1 splice variant characterization uncovers distinct isoform functions and biochemical properties contributing to critical aspects of neurodevelopment, providing previously unknown isoform-level insight into SYNGAP1-related cognitive disorders.

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

High-resolution live imaging reveals how and when the mouse heart first starts to beat during development and how the onset of beating impacts on heart muscle cell maturation and heart formation.

Axon degeneration due to loss of mitochondria is suppressed by CaMKII activity and MAP kinase signaling.

Genetics and biochemical analyses reveal an evolutionarily conserved mechanism to regulate gene isoform expression by mTORC1 and implicate possible gene isoform imbalance in cancer and neurological disorders with mTORC1 pathway dysregulation.