RT Journal Article SR Electronic T1 Multiple Mechanisms for the Potentiation of AMPA Receptor-Mediated Transmission by α-Ca2+/Calmodulin-Dependent Protein Kinase II JF The Journal of Neuroscience JO J. Neurosci. FD Society for Neuroscience SP 4406 OP 4411 DO 10.1523/JNEUROSCI.22-11-04406.2002 VO 22 IS 11 A1 Jean Christophe Poncer A1 José A. Esteban A1 Roberto Malinow YR 2002 UL http://www.jneurosci.org/content/22/11/4406.abstract AB Some forms of activity-dependent synaptic potentiation require the activation of postsynaptic Ca2+/calmodulin-dependent protein kinase II (CaMKII). Activation of CaMKII has been shown to phosphorylate the glutamate receptor 1 subunit of the AMPA receptor (AMPAR), thereby affecting some of the properties of the receptor. Here, a recombinant, constitutively active form of αCaMKII tagged with the fluorescent marker green fluorescent protein (GFP) [αCaMKII1–290–enhanced GFP (EGFP)] was expressed in CA1 pyramidal neurons from hippocampal slices. The changes in glutamatergic transmission onto these cells were analyzed. AMPA but not NMDA receptor-mediated EPSCs were specifically potentiated in infected compared with nearby noninfected neurons. This potentiation was associated with a reduction in the proportion of synapses devoid of AMPARs. In addition, expression of αCaMKII1–290–EGFP increased the quantal size of AMPAR-mediated responses. This effect reflected, at least in part, an increased unitary conductance of the channels underlying the EPSCs. These results reveal that several key features of long-term potentiation of hippocampal glutamatergic synapses are reproduced by the sole activity of αCaMKII.