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Publication : Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors.

First Author  Lee HK Year  2007
Journal  Mol Cell Neurosci Volume  36
Issue  1 Pages  86-94
PubMed ID  17689977 Mgi Jnum  J:126784
Mgi Id  MGI:3761986 Doi  10.1016/j.mcn.2007.06.003
Citation  Lee HK, et al. (2007) Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors. Mol Cell Neurosci 36(1):86-94
abstractText  Phosphorylation of various AMPA receptor subunits can alter synaptic transmission and plasticity at excitatory glutamatergic synapses in the central nervous system. Here, we identified threonine-840 (T840) on the GluR1 subunit of AMPA receptors as a novel phosphorylation site. T840 is phosphorylated by protein kinase C (PKC) in vitro and is a highly turned-over phosphorylation site in the hippocampus. Interestingly, the high basal phosphorylation of T840 in the hippocampus is maintained by a persistent activity of a protein kinase, which is counter-balanced by a basal protein phosphatase activity. To study the function of T840, we generated a line of mutant mice lacking this phosphorylation site using a gene knock-in technique. The mice generated lack T840, in addition to two previously identified phosphorylation sites S831 and S845. Using this mouse, we demonstrate that T840 may regulate synaptic plasticity in an age-dependent manner.
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