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.

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.

In vivo imaging of extracellular signal-regulated kinase activity reveals radial ERK activation patterns that are associated with cell cycle progression in the mouse epidermis.

Two major subtypes of cortical interneurons, the PV and the SST positive cells, causally contribute to the regulation of large-scale state transitions in the cortex.

A neural circuit that can selectively induce sleep-like patterns in small regions of the brain demonstrates how sleep and arousal states may be controlled in local brain regions.

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.

Kindlin-2 co-operates with talin to activate fibronectin-binding integrins on fibroblasts and subsequently induces cell spreading by recruiting paxillin to small, peripheral nascent adhesions.

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

Computational models of gating processes in an ion channel show how stability shifts upon ligand-binding and mutations are reproduced, which highlights mechanistic details and proposes a new role for symmetry in gating.