Commentary Cellscience Reviews Vol 4 No 4 ISSN 1742-8130

Regulated protein degradation facilitates memory reconsolidation

The balance between protein synthesis and degradation is a key aspect of neuronal plasticity. In vivo studies of the molecular determinants of memory also support essential roles for regulated protein degradation and new protein synthesis in memory storage. In a recent study Lee et al. show that ubiquitin-dependent protein degradation underlies memory reconsolidation. The results described in their study support the idea that, during memory retrieval, the ubiquitin proteasome system removes specific proteins from synapses, resulting in the destabilization of the memory trace. Subsequent induction of protein synthesis is then required to re-stabilize and update the memory. The coupling of synaptic activation with induction of the ubiquitin proteasome system may therefore facilitate the reorganization of synaptic proteins required to update and stabilize pre-existing memories.

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