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Regulation of neuronal NMDA receptor is critical in synaptic transmission and plasticity.Protein kinase C (PKC) promotes NMDA receptor (NMDAR) trafficking to the cell surface via interaction with NMDAR-associated proteins (NAPs).Little is known, however, about the NAPs that are critical to PKC-induced NMDAR trafficking.Here, we showed that CaMKII could be a NAP that mediates the potentiation of NMDAR trafficking by PKC.PKC activation promoted the level of autophosphorylated CaMKII and increased association with NMDARs, accompanied by functional NMDAR insertion, at postsynaptic site.This potentiation, along with PKC-induced LTP of AMPA receptor-mediated response, was abolished by CaMKII antagonist or by disturbing the interaction between CaMKII and NR2A or NR2B.Further mutual occluding experiments demonstrated that PKC and CaMKII share a common signaling pathway in the potentiation of NMDAR trafficking and LTP induction.Our results reveal that PKC promotes NMDA receptor trafficking and induces synaptic plasticity through indirectly triggering CaMKII autophosphorylation and subsequent increased association with NMDARs.