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Bidirectional regulation of eEF2 phosphorylation controls synaptic plasticity by decoding neuronal activity patterns.

Patrick K McCamphill¹, Carole A Farah¹, Mina N Anadolu¹

¹Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience

|March 13, 2015

Summary

This study reveals how the Aplysia sensory-motor neuron synapse uses eukaryotic elongation factor 2 (eEF2) to distinguish between spaced and massed serotonin (5-HT) exposure, impacting protein synthesis and synaptic plasticity.

Keywords:

elongation factor 2 facilitation intermediate memory protein kinase C synaptic plasticity translational control

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Area of Science:

Neuroscience
Molecular Biology
Synaptic Plasticity

Background:

Serotonin (5-HT) exposure induces intermediate-term facilitation (ITF) at Aplysia sensory-motor neuron synapses.
Both spaced and massed 5-HT exposure require protein synthesis but not gene transcription for ITF.
Spaced ITF relies on persistent protein kinase A (PKA) activity, while massed ITF depends on persistent protein kinase C (PKC) activity.

Purpose of the Study:

To investigate the role of eukaryotic elongation factor 2 (eEF2) in mediating distinct molecular mechanisms of ITF induced by spaced versus massed 5-HT exposure.
To determine how eEF2 acts as a biochemical sensor for neuronal stimulation patterns.

Main Methods:

Utilized pharmacological and dominant-negative strategies to inhibit eEF2 kinase (eEF2K).
Measured eEF2 phosphorylation levels in response to spaced and massed 5-HT training.
Assessed the impact of eEF2K inhibition on PKC-dependent and PKA-dependent ITF.
Investigated the dependence of 5-HT-induced synaptic strengthening on translation initiation versus elongation.

Main Results:

Massed 5-HT training increased eEF2 phosphorylation in a PKC-dependent manner.
Spaced 5-HT training decreased eEF2 phosphorylation in a PKA-dependent manner.
Inhibition of eEF2K blocked massed 5-HT-dependent increases in eEF2 phosphorylation and PKC-dependent ITF.
Inhibition of eEF2K during spaced training reduced eEF2 phosphorylation and induced ITF.

Conclusions:

Bidirectional regulation of eEF2 phosphorylation is crucial for decoding distinct synaptic activity patterns.
eEF2 acts as a critical sensor, translating stimulation patterns into specific modes of translation regulation.
Massed 5-HT-induced synaptic strengthening primarily requires translation elongation, while spaced training involves translation initiation.