Protein kinase C promotes NMDA receptor trafficking by indirectly triggering CaMKⅡ autophosphorylati

• 作 者: Jing-ZhiYAN[1]Si-QiangREN[1]ZhuoXU[1]WenYAO[1]Shan-HuiWANG[1]Su-YiLIU[1]WeiLU[2]
• 机 构: Department of Neurobiology, Nanjing 210029, China
• 出 处: 中国神经科学学会第九届全国学术会议暨第五届会员代表大会
• 发表日期: 2011年期

　　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.