Yan Z, Hsieh-Wilson L, Feng J, Tomizawa K, Allen P B, Fienberg A A, Nairn A C, Greengard P
Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, New York 10021, USA.
Nat Neurosci. 1999 Jan;2(1):13-7. doi: 10.1038/4516.
Modulation of AMPA-type glutamate channels is important for synaptic plasticity. Here we provide physiological evidence that the activity of AMPA channels is regulated by protein phosphatase 1 (PP-1) in neostriatal neurons and identify two distinct molecular mechanisms of this regulation. One mechanism involves control of PP-1 catalytic activity by DARPP-32, a dopamine- and cAMP-regulated phosphoprotein highly enriched in neostriatum. The other involves binding of PP-1 to spinophilin, a protein that colocalizes PP-1 with AMPA receptors in postsynaptic densities. The results suggest that regulation of anchored PP-1 is important for AMPA-receptor-mediated synaptic transmission and plasticity.
α-氨基-3-羟基-5-甲基-4-异恶唑丙酸（AMPA）型谷氨酸受体通道的调节对突触可塑性至关重要。在此，我们提供生理学证据表明，AMPA受体通道的活性在新纹状体神经元中受蛋白磷酸酶1（PP-1）调控，并确定了这种调控的两种不同分子机制。一种机制涉及由DARPP-32对PP-1催化活性的控制，DARPP-32是一种在新纹状体中高度富集的多巴胺和环磷酸腺苷调节磷蛋白。另一种机制涉及PP-1与亲嗜素的结合，亲嗜素是一种能使PP-1与突触后致密物中的AMPA受体共定位的蛋白质。结果表明，锚定PP-1的调节对AMPA受体介导的突触传递和可塑性很重要。
