Wang L Y, Orser B A, Brautigan D L, MacDonald J F
Department of Physiology, University of Toronto, Canada.
Nature. 1994 May 19;369(6477):230-2. doi: 10.1038/369230a0.
Phosphorylation of glutamate receptors is probably an important mechanism for modulating excitatory transmission. However, there is little direct evidence to indicate which protein phosphatases can dephosphorylate glutamate or other ligand-gated channels, although it is known that protein phosphatases 1 and 2A play a major part in modulating voltage and second-messenger-gated channels. Here we report that in cultured hippocampal neurons, the N-methyl-D-aspartate (NMDA) receptor can be regulated by endogenous and exogenous serine/threonine protein phosphatases. Phosphatase inhibitors enhanced NMDA currents recorded using the perforated patch technique or in cell-attached patches, whereas protein phosphatases 1 or 2A decreased the open probability of these channels in inside-out patches.
谷氨酸受体的磷酸化可能是调节兴奋性传递的重要机制。然而，几乎没有直接证据表明哪些蛋白磷酸酶可以使谷氨酸或其他配体门控通道去磷酸化，尽管已知蛋白磷酸酶1和2A在调节电压门控通道和第二信使门控通道中起主要作用。在此我们报告，在培养的海马神经元中，N-甲基-D-天冬氨酸（NMDA）受体可受内源性和外源性丝氨酸/苏氨酸蛋白磷酸酶的调节。磷酸酶抑制剂增强了使用穿孔膜片钳技术或在细胞贴附膜片中记录的NMDA电流，而蛋白磷酸酶1或2A降低了内面向外膜片中这些通道的开放概率。
