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The Journal of Neuroscience, March 15, 2002, 22(6):2153-2164
Rapid Synaptic Remodeling by Protein Kinase C: Reciprocal Translocation of NMDA Receptors and Calcium/Calmodulin-Dependent Kinase II
Dan K. Fong, Anuradha Rao, F. Thomas Crump, and Ann Marie Craig Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110
In contrast to the rapid regulation of AMPA receptors, previous evidence has supported the idea that the synaptic density of NMDA-type glutamate receptors is fairly static, modulated only over a long time scale in a homeostatic manner. We report here that selective activation of protein kinase C (PKC) with phorbol esters induces a rapid dispersal of NMDA receptors from synaptic to extrasynaptic plasma membrane in cultured rat hippocampal neurons. PKC activation induced a simultaneous translocation of calcium/calmodulin-dependent kinase II (CaMKII) to synapses but no change in spine number, presynaptic terminal number, or the distribution of AMPA receptors or the synaptic scaffolding protein PSD-95. PKC-induced accumulation of CaMKII was dependent on filamentous actin, whereas dispersal of NMDA receptors occurred by a different mechanism independent of actin or CaMKII. Consistent with the decrease in synaptic density of NMDA receptors, phorbol ester pretreatment reduced excitotoxicity. These results reveal a surprisingly dynamic nature to the molecular composition and functional properties of glutamatergic postsynaptic specializations.
Key words: postsynaptic density; NMDA receptors; calcium/calmodulin-dependent kinase II; protein kinase C; synaptogenesis; synaptic plasticity; hippocampal neurons
Copyright © 2002 Society for Neuroscience 0270-6474/02/2262153-12$05.00/0
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