Memory can last a lifetime, yet synaptic contacts that contribute to the storage of memory are composed of proteins that have much shorter lifetimes. A physiological model of memory formation, long-term potentiation (LTP), has a late protein-synthesis-dependent phase (L-LTP) that can last for many hours in slices or even for days in vivo. Could the activity-dependent synthesis of new proteins account for the persistence of L-LTP and memory? Here, we examine the proposal that a selfsustaining regulation of translation can form a bistable switch that can persistently regulate the onsite synthesis of plasticity-related proteins. We show that an aCaMKII-CPEB1 molecular pair can operate as a bistable switch. Our results imply that L-LTP should produce an increase in the total amount of aCaMKII at potentiated synapses. This study also proposes an explanation for why the application of protein synthesis and aCaMKII inhibitors at the induction and maintenance phases of L-LTP result in very different outcomes.

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Sharp central venous recanalization using the transseptal needle is feasible technique in patients who failed standard recanalization procedures. The potential high risk of complications necessitates thorough awareness of anatomy and proper technical preparedness.

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