Binding of the inward rectifier K+ channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation

Noam A. Cohen, Jay E. Brenman, Solomon H. Snyder, David S. Bredt

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)759-767
Number of pages9
JournalNeuron
Volume17
Issue number4
DOIs
StatePublished - Oct 1996

ASJC Scopus subject areas

  • Neuroscience(all)

Fingerprint Dive into the research topics of 'Binding of the inward rectifier K<sup>+</sup> channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation'. Together they form a unique fingerprint.

Cite this