Abstract
At excitatory synapses of hippocampal CA1 pyramidal neurons, the activation of postsynaptic calcium/calmodulin-dependent protein kinase II (CaMKII) by calmodulin (CaM) during a brief high magnitude elevation of intracellular Ca2+ concentration ([Ca]i) results in LTP induction. Conversely, the same protein, CaM, activates PP2B (calcineurin) during a prolonged modest rise of [Ca]i that induces LTD [1,2]. We would like to understand the mechanism by which the same protein (CaM) can activate one process while suppressing the other?
Highlights
At excitatory synapses of hippocampal CA1 pyramidal neurons, the activation of postsynaptic calcium/calmodulin-dependent protein kinase II (CaMKII) by calmodulin (CaM) during a brief high magnitude elevation of intracellular Ca2+ concentration ([Ca2+]i) results in LTP induction
Ng is a 78 amino acid neuronal protein enriched in CA1 pyramidal neurons that interacts with the C-terminal lobe of CaM both in the presence and absence of Ca2+ [3]
Once autophosphorylated at Thr286, CaMKII becomes resistant to the action of Ng and binds CaM with much higher affinity than PP2B [3,4]
Summary
At excitatory synapses of hippocampal CA1 pyramidal neurons, the activation of postsynaptic calcium/calmodulin-dependent protein kinase II (CaMKII) by calmodulin (CaM) during a brief high magnitude elevation of intracellular Ca2+ concentration ([Ca2+]i) results in LTP induction. Address: Department of Neurobiology and Anatomy, University of Texas Medical School, 6431 Fannin, Houston, TX 77030, USA Email: Yoshihisa Kubota* - yoshihisa.kubota@uth.tmc.edu * Corresponding author from Seventeenth Annual Computational Neuroscience Meeting: CNS*2008 Portland, OR, USA. Published: 11 July 2008 BMC Neuroscience 2008, 9(Suppl 1):P108 doi:10.1186/1471-2202-9-S1-P108
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