ArticleScience advances2026
CaMKIIα holoenzymes self-organize into chain-like mesoscale clusters.
Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Calcium- and calmodulin-dependent protein kinase II (CaMKII) is highly enriched in dendritic spines at concentrations comparable to those of cytoskeletal proteins and plays a central role in synaptic plasticity. During long-term potentiation, CaMKIIα further accumulates in spines. However, the mechanisms governing its higher-order organization remain poorly understood. Here, we use high-speed atomic force microscopy to visualize interholoenzyme interaction of CaMKIIα at mesoscopic scales (5 to 500 nanometers). Under freely diffusible conditions, CaMKIIα holoenzymes do not form stable clusters. In contrast, when spatially confined, they assemble into chain-like clusters mediated by kinase-domain interactions. These clusters expand upon activation, concomitant with the dissociation of the regulatory segment. Notably, the CaMKIIα Pro
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