Abstract
The ubiquitin-proteasome pathway is essential for long-term synaptic plasticity, but its exact roles remain unclear. Previously we established that proteasome inhibition increased the early, induction part of late-phase long-term potentiation (L-LTP) but blocks the late, maintenance part. Our prior work also showed that the proteasome modulates components of the mammalian target of rapamycin pathway for translation. In this study, we tested the possible role of the proteasome in regulating the cytoplasmic polyadenylation signaling required for translation during L-LTP. We found that a polyadenylation inhibitor cordycepin diminishes the enhancement of early L-LTP mediated by proteasome inhibition. Furthermore, blocking Aurora-A kinase and calcium-calmodulin-dependent kinase II reduces the increase in early L-LTP brought about by proteasome inhibition. Our results suggest a link between polyadenylation-mediated translational control and protein degradation during induction of long-term synaptic plasticity.