Interaction between αCaMKII and GluN2B controls ERK-dependent plasticity

F. El Gaamouch, A. Buisson, O. Moustie, M. Lemieux, S. Labrecque, B. Bontempi, P. De Koninck, O. Nicole
Journal of Neuroscience. 2012-08-01; 32(31): 10767-10779
DOI: 10.1523/JNEUROSCI.5622-11.2012

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1. J Neurosci. 2012 Aug 1;32(31):10767-79. doi: 10.1523/JNEUROSCI.5622-11.2012.

Interaction between αCaMKII and GluN2B controls ERK-dependent plasticity.

El Gaamouch F(1), Buisson A, Moustié O, Lemieux M, Labrecque S, Bontempi B, De
Koninck P, Nicole O.

Author information:
(1)Université de Caen-Basse Normandie, CNRS UMR 6232, CINAPS-PSY, 14 000 Caen,
France.

Understanding how brief synaptic events can lead to sustained changes in synaptic
structure and strength is a necessary step in solving the rules governing
learning and memory. Activation of ERK1/2 (extracellular signal regulated protein
kinase 1/2) plays a key role in the control of functional and structural synaptic
plasticity. One of the triggering events that activates ERK1/2 cascade is an NMDA
receptor (NMDAR)-dependent rise in free intracellular Ca(2+) concentration.
However the mechanism by which a short-lasting rise in Ca(2+) concentration is
transduced into long-lasting ERK1/2-dependent plasticity remains unknown. Here we
demonstrate that although synaptic activation in mouse cultured cortical neurons
induces intracellular Ca(2+) elevation via both GluN2A and GluN2B-containing
NMDARs, only GluN2B-containing NMDAR activation leads to a long-lasting ERK1/2
phosphorylation. We show that αCaMKII, but not βCaMKII, is critically involved in
this GluN2B-dependent activation of ERK1/2 signaling, through a direct
interaction between GluN2B and αCaMKII. We then show that interfering with
GluN2B/αCaMKII interaction prevents synaptic activity from inducing ERK-dependent
increases in synaptic AMPA receptors and spine volume. Thus, in a developing
circuit model, the brief activity of synaptic GluN2B-containing receptors and the
interaction between GluN2B and αCaMKII have a role in long-term plasticity via
the control of ERK1/2 signaling. Our findings suggest that the roles that these
major molecular elements have in learning and memory may operate through a common
pathway.

DOI: 10.1523/JNEUROSCI.5622-11.2012
PMID: 22855824 [Indexed for MEDLINE]


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