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The Journal of Neuroscience, September 15, 2001, 21(18):7053-7062

Mitogen-Activated Protein Kinase Regulates Early Phosphorylation and Delayed Expression of Ca²⁺/Calmodulin-Dependent Protein Kinase II in Long-Term Potentiation

Maria Grazia Giovannini^{1, 5}, Robert D. Blitzer^{1, 2, 4}, Tony Wong², Kichiemon Asoma², Panayiotis Tsokas¹, John H. Morrison³, Ravi Iyengar¹, and Emmanuel M. Landau^{1, 2, 4}

Departments of ¹ Pharmacology and ² Psychiatry, and ³ Neurobiology of Aging Laboratories, Mount Sinai School of Medicine, New York, New York 10029, ⁴ Psychiatry Service, Bronx Veterans Affairs Medical Center, Bronx, New York 10468, and ⁵ Dipartimento di Farmacologia Preclinica e Clinica, Universitá di Firenze, Firenze, Italy

Activation of mitogen-activated protein kinase (MAPK) and Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) are required for numerous forms of neuronal plasticity, including long-term potentiation (LTP). We induced LTP in rat hippocampal area CA1 using theta-pulse stimulation (TPS) paired with -adrenergic receptor activation [isoproterenol (ISO)], a protocol that may be particularly relevant to normal patterns of hippocampal activity during learning. This stimulation resulted in a transient phosphorylation of p42 MAPK, and the resulting LTP was MAPK dependent. In addition, CaMKII was regulated in two, temporally distinct ways after TPS-ISO: a transient rise in the fraction of phosphorylated CaMKII and a subsequent persistent increase in CaMKII expression. The increases in MAPK and CaMKII phosphorylation were strongly colocalized in the dendrites and cell bodies of CA1 pyramidal cells, and both the transient phosphorylation and delayed expression of CaMKII were prevented by inhibiting p42/p44 MAPK. These results establish a novel bimodal regulation of CaMKII by MAPK, which may contribute to both post-translational modification and increased gene expression.

Key words: long-term potentiation; mitogen-activated protein kinase; Erk; Ca²⁺/calmodulin-dependent protein kinase II; -adrenergic receptors; rat hippocampus; phosphorylation; protein synthesis

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Copyright © 2001 Society for Neuroscience  0270-6474/01/21187053-10$05.00/0

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