Long-term memory consolidation depends on proteasome activity in the crab Chasmagnathus

Neuroscience. 2007 Jun 15;147(1):46-52. doi: 10.1016/j.neuroscience.2007.04.022. Epub 2007 May 22.

Abstract

Long-term memory formation depends on protein and mRNA synthesis that subserves synaptic reorganization. The removal of pre-existing inhibitory proteins by the ubiquitin-proteasome system (UPS) is proposed as a crucial step to support these modifications. The activation of the constitutive transcription factor nuclear factor kappaB (NF-kappaB) depends on the degradation of the inhibitor of NF-kappaB (IkappaB) by the UPS. Here we study the effect of a UPS inhibitor, MG132, on long-term memory consolidation and NF-kappaB activation in the learning paradigm of the crab Chasmagnathus, a model in which this transcription factor plays a key role. Here we found that administration of MG132 interferes with long-term memory but not with short-term memory, and no facilitatory effects were found. Then we studied the effect of the UPS inhibitor on NF-kappaB pathway, finding that MG132 blocks the activation of NF-kappaB induced by training. These results suggest that the UPS is necessary for long-term memory consolidation, allowing for the activation of NF-kappaB as one of the target molecular pathways.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brachyura / enzymology*
  • Conditioning, Classical / drug effects
  • Conditioning, Classical / physiology*
  • Cysteine Proteinase Inhibitors / pharmacology
  • Dose-Response Relationship, Drug
  • Leupeptins / pharmacology
  • Male
  • Memory / drug effects
  • Memory / physiology*
  • Motor Activity
  • NF-kappa B / metabolism*
  • Neuronal Plasticity / drug effects
  • Neuronal Plasticity / physiology
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteasome Inhibitors
  • Time Factors
  • Ubiquitin / drug effects
  • Ubiquitin / metabolism

Substances

  • Cysteine Proteinase Inhibitors
  • Leupeptins
  • NF-kappa B
  • Proteasome Inhibitors
  • Ubiquitin
  • Proteasome Endopeptidase Complex
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde