Abstract
Using targeted mouse mutants and pharmacologic inhibition of alphaCaMKII, we demonstrate that the alphaCaMKII protein, but not its activation, autophosphorylation or its ability to phosphorylate synapsin I, is required for normal short-term presynaptic plasticity. Furthermore, alphaCaMKII regulates the number of docked vesicles independent of its ability to be activated. These results indicate that alphaCaMKII has a nonenzymatic role in short-term presynaptic plasticity at hippocampal CA3-CA1 synapses.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Analysis of Variance
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Animals
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Calcium-Calmodulin-Dependent Protein Kinase Type 2 / genetics
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Calcium-Calmodulin-Dependent Protein Kinase Type 2 / physiology*
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Electric Stimulation
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Enzyme Activation / genetics
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Excitatory Postsynaptic Potentials / genetics
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Hippocampus / cytology*
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Mice
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Mice, Inbred C57BL
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Mice, Transgenic
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Microscopy, Electron, Transmission / methods
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Mutagenesis / physiology
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Neuronal Plasticity / physiology*
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Neurons / physiology*
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Neurons / radiation effects
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Patch-Clamp Techniques / methods
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Phosphorylation
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Presynaptic Terminals / physiology*
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Presynaptic Terminals / ultrastructure
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Synapses / physiology*
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Synapses / ultrastructure
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Synapsins / metabolism
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Synaptic Transmission / genetics
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Synaptic Transmission / physiology*
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Synaptic Vesicles / physiology
Substances
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Synapsins
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Calcium-Calmodulin-Dependent Protein Kinase Type 2