Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors.

@article{Yakel1995IdentificationOA,
  title={Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors.},
  author={Jerrel L Yakel and Prabakhar Vissavajjhala and Victor A. Derkach and Debra A. Brickey and Thomas R. Soderling},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 5},
  pages={1376-80}
}
Glutamate receptor ion channels are colocalized in postsynaptic densities with Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II), which can phosphorylate and strongly enhance non-N-methyl-D-aspartate (NMDA) glutamate receptor current. In this study, CaM-kinase II enhanced kainate currents of expressed glutamate receptor 6 in 293 cells and of wild-type glutamate receptor 1, but not the Ser-627 to Ala mutant, in Xenopus oocytes. A synthetic peptide corresponding to residues 620-638 in… CONTINUE READING
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