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    Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation

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    9324.pdf (472.5Kb)
    Date
    2004-10-20
    Author
    Otmakhov, Nikolai  Concept link
    Tao-Cheng, Jung-Hwa  Concept link
    Carpenter, Stephen  Concept link
    Asrican, Brent  Concept link
    Dosemeci, Ayse  Concept link
    Reese, Thomas S.  Concept link
    Lisman, John E.  Concept link
    Metadata
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    Citable URI
    https://hdl.handle.net/1912/2961
    As published
    https://doi.org/10.1523/JNEUROSCI.2350-04.2004
    DOI
    10.1523/JNEUROSCI.2350-04.2004
    Keyword
     Protein kinase; Postsynaptic density; Imaging; Synapse; LTP long-term potentiation; EM; Tissue culture; Fluorescence 
    Abstract
    Calcium/calmodulin-dependent protein kinase II (CaMKII) is a leading candidate for a synaptic memory molecule because it is persistently activated after long-term potentiation (LTP) induction and because mutations that block this persistent activity prevent LTP and learning. Previous work showed that synaptic stimulation causes a rapidly reversible translocation of CaMKII to the synaptic region. We have now measured green fluorescent protein (GFP)-CaMKIIα translocation into synaptic spines during NMDA receptor-dependent chemical LTP (cLTP) and find that under these conditions, translocation is persistent. Using red fluorescent protein as a cell morphology marker, we found that there are two components of the persistent accumulation. cLTP produces a persistent increase in spine volume, and some of the increase in GFP-CaMKIIα is secondary to this volume change. In addition, cLTP results in a dramatic increase in the bound fraction of GFP-CaMKIIα in spines. To further study the bound pool, immunogold electron microscopy was used to measure CaMKIIα in the postsynaptic density (PSD), an important regulator of synaptic function. cLTP produced a persistent increase in the PSD-associated pool of CaMKIIα. These results are consistent with the hypothesis that CaMKIIα accumulation at synapses is a memory trace of past synaptic activity.
    Description
    Author Posting. © Society for Neuroscience, 2004. This article is posted here by permission of Society for Neuroscience for personal use, not for redistribution. The definitive version was published in Journal of Neuroscience 24 (2004): 9324-9331, doi:10.1523/JNEUROSCI.2350-04.2004.
    Collections
    • Program in Molecular Physiology
    Suggested Citation
    Journal of Neuroscience 24 (2004): 9324-9331
     

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