Lan J Y, Skeberdis V A, Jover T, Grooms S Y, Lin Y, Araneda R C, Zheng X, Bennett M V, Zukin R S
Department of Neuroscience, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Nat Neurosci. 2001 Apr;4(4):382-90. doi: 10.1038/86028.
Regulation of neuronal N-methyl-D-aspartate receptors (NMDARs) by protein kinases is critical in synaptic transmission. However, the molecular mechanisms underlying protein kinase C (PKC) potentiation of NMDARs are uncertain. Here we demonstrate that PKC increases NMDA channel opening rate and delivers new NMDA channels to the plasma membrane through regulated exocytosis. PKC induced a rapid delivery of functional NMDARs to the cell surface and increased surface NR1 immunofluorescence in Xenopus oocytes expressing NMDARs. PKC potentiation was inhibited by botulinum neurotoxin A and a dominant negative mutant of soluble NSF-associated protein (SNAP-25), suggesting that receptor trafficking occurs via SNARE-dependent exocytosis. In neurons, PKC induced a rapid delivery of functional NMDARs, assessed by electrophysiology, and an increase in NMDAR clusters on the surface of dendrites and dendritic spines, as indicated by immunofluorescence. Thus, PKC regulates NMDAR channel gating and trafficking in recombinant systems and in neurons, mechanisms that may be relevant to synaptic plasticity.
蛋白激酶对神经元N-甲基-D-天冬氨酸受体(NMDARs)的调节在突触传递中至关重要。然而,蛋白激酶C(PKC)增强NMDARs的分子机制尚不清楚。在此我们证明,PKC可提高NMDA通道的开放速率,并通过受调控的胞吐作用将新的NMDA通道转运至质膜。PKC诱导功能性NMDARs快速转运至细胞表面,并增加了表达NMDARs的非洲爪蟾卵母细胞表面的NR1免疫荧光。肉毒杆菌神经毒素A和可溶性NSF相关蛋白(SNAP-25)的显性负性突变体可抑制PKC的增强作用,这表明受体转运是通过依赖SNARE的胞吐作用发生的。在神经元中,通过电生理学评估发现PKC诱导功能性NMDARs快速转运,免疫荧光显示树突和树突棘表面的NMDAR簇增加。因此,PKC在重组系统和神经元中调节NMDAR通道的门控和转运,这些机制可能与突触可塑性有关。