@article{565112378ac3408087119e53c2a5d943,
title = "Binding of the inward rectifier K+ channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation",
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.",
author = "Cohen, {Noam A.} and Brenman, {Jay E.} and Snyder, {Solomon H.} and Bredt, {David S.}",
note = "Funding Information: We thank David Sabatini, Paul Worley, and John Forsayeth for advice regarding experimental design, Andrew Mammen, Katherine Roche, and Richard Huganir for expert technical advice on phosphorylation, Miriam Freedman and Irfan Quereshi for expert technical assistance, Deborah Nelson for the Kir 2.1 and 3.1 clones, and Morgan Sheng for the PSD-95 expression vector. This work was supported by United States Public Health Service Grant DA-00266, a Research Scientist Award MH-18501 to S. H. S., R01NS34822 to D. S. B., Training Grant MH-10341 to N. A. C., an American Heart Association predoctoral fellowship to J. E. B., and grants from the W. M. Keck Foundation and Lucille P. Markey Charitable Trust. Correspondence should be addressed to D. S. B. ",
year = "1996",
month = oct,
doi = "10.1016/S0896-6273(00)80207-X",
language = "English (US)",
volume = "17",
pages = "759--767",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "4",
}