Activity drives local CaMKII synthesis and subcellular localization via autophosphorylation-dependent pathways

Spaced stimulation at the Drosophila larval neuromuscular junction rapidly increases presynaptic CaMKII via local translation, requiring CaMKII T287 autophosphorylation and distinct 3'UTR-dependent localization.

• Why it matters: Presynaptic activity-dependent protein synthesis and how it shapes CaMKII pools are poorly understood, limiting insight into mechanisms of long-lasting synaptic plasticity.
• What they did: Using presynaptic-specific tagging of endogenous CaMKII, the study tests local translation requirements and shows dependence on the distal CaMKII mRNA 3'UTR and on PI3K/Akt/mTor signaling activated by CaMKII T287 autophosphorylation.
• The result: A T287D phosphomimetic localizes to the synaptic membrane, and pulse-chase experiments indicate newly synthesized CaMKII localizes differently than pre-existing CaMKII, implying spatially distinct CaMKII populations.

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