Neuron
Volume 17, Issue 4, October 1996, Pages 759-767
Journal home page for Neuron

Article
Binding of the Inward Rectifier K+ Channel Kir 2.3 to PSD-95 Is Regulated by Protein Kinase A Phosphorylation

https://doi.org/10.1016/S0896-6273(00)80207-XGet rights and content
Under a Creative Commons license
open archive

Abstract

Dynamic regulation of ion channel interactions with the cytoskeleton mediates aspects of synaptic plasticity, yet mechanisms for this process are largely unknown. Here, we report that two inwardly rectifying K+ channels, Kir 2.1 and 2.3, bind to PSD-95, a cytoskeletal protein of postsynaptic densities that clusters NMDA receptors and voltage-dependent K+ channels. Kir 2.3 colocalizes with PSD-95 in neuronal populations in forebrain, and a PSD-95/Kir 2.3 complex occurs in hippocampus. Within the C-terminal tail of Kir 2.3, a serine residue critical for interaction with PSD-95, is also a substrate for phosphorylation by protein kinase A (PKA). Stimulation of PKA in intact cells causes rapid dissociation of the channel from PSD-95. This work identifies a physiological mechanism for regulating ion channel interactions with the postsynaptic density.

Cited by (0)