We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP.
- Authors
Blitzer, R D; Connor, J H; Brown, G P; Wong, T; Shenolikar, S; Iyengar, R; Landau, E M
- Abstract
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.
- Publication
Science (New York, N.Y.), 1998, Vol 280, Issue 5371, p1940
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.280.5371.1940