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The Journal of Neuroscience, February 23, 2005, 25(8):1979-1984; doi:10.1523/JNEUROSCI.5132-04.2005

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Persistent Phosphorylation by Protein Kinase M Maintains Late-Phase Long-Term Potentiation

Peter Serrano, Yudong Yao, and Todd Charlton Sacktor

Departments of Physiology, Pharmacology, and Neurology, State University of New York Downstate Medical Center, Brooklyn, New York 11203

Protein kinase M (PKM), an autonomously active atypical PKC isoform, is both necessary and sufficient for enhanced synaptic transmission during long-term potentiation (LTP) maintenance. LTP, however, evolves through several temporal phases, which may be mediated by distinct molecular mechanisms of potentiation. Here, we determined the specific phase of LTP maintained by PKM. Using a selective, cell-permeable -pseudosubstrate inhibitor at concentrations that block potentiation produced by postsynaptic perfusion of PKM, we inhibited PKM activity at various times after tetanization of Schaffer collateral/commissural-CA1 synapses. Inhibition of PKM did not affect baseline AMPA receptor-mediated synaptic transmission or an early phase of LTP. In contrast, the inhibitor reversed established LTP when applied 1, 3, or 5 h after tetanic stimulation. Control nontetanized pathways within the hippocampal slices were unaffected. An inactive scrambled version of the peptide had no effect on LTP. Thus, persistent, increased phosphorylation by PKM specifically maintains the late phase of LTP.

Key words: PKM; PKC; long-term potentiation; memory; ZIP; PKC

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Received June 22, 2004; revised January 12, 2005; accepted January 12, 2005.

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