A role for the Ras signalling pathway in synaptic transmission and long-term memory

Nature. 1997 Nov 20;390(6657):281-6. doi: 10.1038/36849.

Abstract

Members of the Ras subfamily of small guanine-nucleotide-binding proteins are essential for controlling normal and malignant cell proliferation as well as cell differentiation. The neuronal-specific guanine-nucleotide-exchange factor, Ras-GRF/CDC25Mm, induces Ras signalling in response to Ca2+ influx and activation of G-protein-coupled receptors in vitro, suggesting that it plays a role in neurotransmission and plasticity in vivo. Here we report that mice lacking Ras-GRF are impaired in the process of memory consolidation, as revealed by emotional conditioning tasks that require the function of the amygdala; learning and short-term memory are intact. Electrophysiological measurements in the basolateral amygdala reveal that long-term plasticity is abnormal in mutant mice. In contrast, Ras-GRF mutants do not reveal major deficits in spatial learning tasks such as the Morris water maze, a test that requires hippocampal function. Consistent with apparently normal hippocampal functions, Ras-GRF mutants show normal NMDA (N-methyl-D-aspartate) receptor-dependent long-term potentiation in this structure. These results implicate Ras-GRF signalling via the Ras/MAP kinase pathway in synaptic events leading to formation of long-term memories.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Amygdala / physiology
  • Animals
  • Avoidance Learning
  • Brain / pathology
  • Brain / physiology
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / physiology*
  • Conditioning, Classical
  • Electrophysiology
  • Fear
  • Hippocampus / physiology
  • Maze Learning
  • Memory / physiology*
  • Mice
  • Mice, Inbred C57BL
  • Mutagenesis
  • Neuronal Plasticity
  • Phosphoprotein Phosphatases / genetics
  • Phosphoprotein Phosphatases / physiology*
  • Signal Transduction*
  • Spatial Behavior
  • Synapses / physiology*
  • ras Proteins / physiology*
  • ras-GRF1

Substances

  • Cell Cycle Proteins
  • ras-GRF1
  • Phosphoprotein Phosphatases
  • ras Proteins