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
Language
- eng
Conference Location
- United States