Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Blitzer, RD; Connor, JH; Brown, GP; Wong, T; Shenolikar, S; Iyengar, R; Landau, EM

Published Date

  • June 19, 1998

Published In

Volume / Issue

  • 280 / 5371

Start / End Page

  • 1940 - 1942

PubMed ID

  • 9632393

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.280.5371.1940


  • eng

Conference Location

  • United States