1. Protein Kinase C Promotes N-Methyl-D-aspartate (NMDA) Receptor Trafficking by Indirectly Triggering Calcium/ Calmodulin-dependent Protein Kinase II (CaMKII) Autophosphorylation.
- Author
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Jing-Zhi Yan, Zhuo Xu, Si-Qiang Ren, Bin Hu, Wen Yao, Shan-Hui Wang, Su-Yi Liu, and Wei Lu
- Subjects
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PROTEIN kinases , *PHOSPHORYLATION , *CELL membranes , *CALCIUM , *NEURAL transmission - Abstract
Regulation of neuronal NMDA receptor (NMDAR) is critical in synaptic transmission and plasticity. Protein kinase C (PKC) promotes 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 calcium/calmodulin-dependent protein kinase II (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 sites. This potentiation, along with PKC-induced long term potentiation of the AMPA receptor-mediated response, was abolished by CaMI(II antagonist or by disturbing the interaction between CaMI(II and NR2A or NR2B. Further mutual occlusion experiments demonstrated that PKC and CaMKII share a common signaling pathway in the potentiation of NMDAR trafficking and longterm potentiation (LTP) induction. Our results revealed that PKC promotes NMDA receptor trafficking and induces synaptic plasticity through indirectly triggering CaMKII autophosphorylation and subsequent increased association with NMDARs. [ABSTRACT FROM AUTHOR]
- Published
- 2011
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