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Science 19 June 1998:
Vol. 280. no. 5371, pp. 1940 - 1943
DOI: 10.1126/science.280.5371.1940
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Reports

Gating of CaMKII by cAMP-Regulated Protein Phosphatase Activity During LTP

Robert D. Blitzer, * John H. Connor, George P. Brown, Tony Wong, Shirish Shenolikar, Ravi Iyengar, Emmanuel M. Landau

Long-term potentiation (LTP) at the Schaffer collateral-CA1 synapse involves interacting signaling components, including calcium (Ca2+)/calmodulin-dependent protein kinase II (CaMKII) and cyclic adenosine monophosphate (cAMP) pathways. Postsynaptic injection of thiophosphorylated inhibitor-1 protein, a specific inhibitor of protein phosphatase-1 (PP1), substituted for cAMP pathway activation in LTP. Stimulation that induced LTP triggered cAMP-dependent phosphorylation of endogenous inhibitor-1 and a decrease in PP1 activity. This stimulation also increased phosphorylation of CaMKII at Thr286 and Ca2+-independent CaMKII activity in a cAMP-dependent manner. The blockade of LTP by a CaMKII inhibitor was not overcome by thiophosphorylated inhibitor-1. Thus, the cAMP pathway uses PP1 to gate CaMKII signaling in LTP.

R. D. Blitzer, Bronx VA Medical Center and Department of Psychiatry, Mount Sinai School of Medicine, New York, NY 10029, USA.
J. H. Connor and S. Shenolikar, Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27712, USA.
G. P. Brown and R. Iyengar, Department of Pharmacology, Mount Sinai School of Medicine, New York, NY 10029, USA.
T. Wong, Department of Psychiatry, Mount Sinai School of Medicine, New York, NY 10029, USA.
E. M. Landau, Bronx VA Medical Center and Departments of Psychiatry and Pharmacology, Mount Sinai School of Medicine, New York, NY 10029, USA.
*   To whom correspondence should be addressed. E-mail: rb2{at}doc.mssm.edu

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