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  Postsynaptic decoding of neural activity: eEF2 as a biochemical sensor coupling miniature synaptic transmission to local protein synthesis

Sutton, M. A., Taylor, A. M., Ito, H. T., Pham, A., & Schuman, E. M. (2007). Postsynaptic decoding of neural activity: eEF2 as a biochemical sensor coupling miniature synaptic transmission to local protein synthesis. Neuron, 55(4), 648-661. doi:10.1016/j.neuron.2007.07.030.

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Sutton, M. A., Author
Taylor, A. M., Author
Ito, H. T., Author
Pham, A., Author
Schuman, Erin M.1, Author              
Affiliations:
1Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              

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Free keywords: Action Potentials/drug effects/*physiology/radiation effects Analysis of Variance Animals Animals, Newborn Cells, Cultured Dendrites/*physiology Diagnostic Imaging Eukaryotic Initiation Factor-2/genetics/*metabolism Excitatory Amino Acid Antagonists/pharmacology Excitatory Postsynaptic Potentials Green Fluorescent Proteins/metabolism Hippocampus/cytology Neurons/*cytology/*physiology Patch-Clamp Techniques/methods Protein Biosynthesis Rats Synaptic Transmission/*physiology Tetrodotoxin/pharmacology Transfection/methods
 Abstract: Activity-dependent regulation of dendritic protein synthesis is critical for enduring changes in synaptic function, but how the unique features of distinct activity patterns are decoded by the dendritic translation machinery remains poorly understood. Here, we identify eukaryotic elongation factor-2 (eEF2), which catalyzes ribosomal translocation during protein synthesis, as a biochemical sensor in dendrites that is specifically and locally tuned to the quality of neurotransmission. We show that intrinsic action potential (AP)-mediated network activity in cultured hippocampal neurons maintains eEF2 in a relatively dephosphorylated (active) state, whereas spontaneous neurotransmitter release (i.e., miniature neurotransmission) strongly promotes the phosphorylation (and inactivation) of eEF2. The regulation of eEF2 phosphorylation is responsive to bidirectional changes in miniature neurotransmission and is controlled locally in dendrites. Finally, direct spatially controlled inhibition of eEF2 phosphorylation induces local translational activation, suggesting that eEF2 is a biochemical sensor that couples miniature synaptic events to local translational suppression in neuronal dendrites.

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 Dates: 2007-08-19
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: Other: 17698016
DOI: 10.1016/j.neuron.2007.07.030
ISSN: 0896-6273 (Print)0896-6273 (Linking)
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Title: Neuron
Source Genre: Journal
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Pages: - Volume / Issue: 55 (4) Sequence Number: - Start / End Page: 648 - 661 Identifier: -