Soderling T R
Vollum Institute, Oregon Health Sciences University, Portland 97201.
Mol Cell Biochem. 1993 Nov;127-128:93-101. doi: 10.1007/BF01076760.
Numerous studies over the past decade have established a role(s) for protein phosphorylation in modulation of synaptic efficiency. This article reviews this data and focuses on putative functions of Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II) which is highly concentrated at these synapses which utilize glutamate as the neurotransmitter. Evidence is presented that CaM-kinase II can phosphorylate these glutamate receptor/ion channels and enhance the ion current flowing through them. This may contribute to mechanisms of synaptic plasticity that are important in cellular paradigms of learning and memory such as long-term potentiation in the hippocampus.
在过去十年中,大量研究证实了蛋白质磷酸化在调节突触效率方面的作用。本文回顾了这些数据,并重点关注钙/钙调蛋白依赖性蛋白激酶II(CaM激酶II)的假定功能,该激酶高度集中在以谷氨酸作为神经递质的这些突触中。有证据表明,CaM激酶II可以使这些谷氨酸受体/离子通道磷酸化,并增强流过它们的离子电流。这可能有助于在学习和记忆的细胞模型(如海马体中的长时程增强)中起重要作用的突触可塑性机制。