Jonas E A, Kaczmarek L K
Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06520, USA.
Curr Opin Neurobiol. 1996 Jun;6(3):318-23. doi: 10.1016/s0959-4388(96)80114-0.
Studies of the role of protein phosphorylation in the modulation of neuronal excitability are beginning to identify specific sites on ion channels that are substrates for serine/threonine kinases and that contribute to short-term and long-term regulation of current amplitude and kinetics. In addition, it is becoming apparent that phosphorylation of tyrosine residues may produce acute changes in the characteristics of ion channels. These recent findings are best illustrated by examining the Shaker superfamily of potassium channels.
关于蛋白质磷酸化在调节神经元兴奋性中作用的研究,开始确定离子通道上作为丝氨酸/苏氨酸激酶作用底物的特定位点,这些位点有助于对电流幅度和动力学进行短期和长期调节。此外,越来越明显的是,酪氨酸残基的磷酸化可能使离子通道特性产生急性变化。通过研究钾通道的Shaker超家族可以很好地说明这些最新发现。