Phosphorylation and modulation of a Kainate receptor (GluR6) by cAMP-dependent protein kinase
作者： L. Wang , F. Taverna , X. Huang , J. MacDonald , D. Hampson
关键词: Phosphorylation 、 Biology 、 Cell biology 、 Kainate receptor 、 Protein kinase A 、 Protein phosphorylation 、 Receptor 、 Long-term potentiation 、 Glutamate receptor 、 Biochemistry 、 Metabotropic glutamate receptor
摘要: Ligand-gated ion channels gated by glutamate constitute the major excitatory neurotransmitter system in mammalian brain. The functional modulation of GluR6, a kainate-activated receptor, adenosine 3',5'-monophosphate-dependent protein kinase A (PKA) was examined with receptors expressed human embryonic kidney cells. Kainate-evoked currents underwent rapid desensitization that blocked lectins. Kainate were potentiated intracellular perfusion PKA, and this potentiation co-application an inhibitory peptide. Site-directed mutagenesis used to identify site or sites phosphorylation on GluR6. Although two serine residues, Ser684 Ser666, required for complete abolition PKA-induced potentiation, may be preferred native GluR6 receptor complexes. These results indicate function can directly modulated suggest dynamic regulation could associated some forms learning memory
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