Regulation of GluA1 α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor function by protein kinase C at serine-818 and threonine-840.

摘要: Three residues within the AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor subunit GluA1 C terminus (Ser818, Ser831, Thr840) can be phosphorylated by Ca2+/phospholipid-dependent protein kinase (PKC). Here, we show that PKC phosphorylation of Ser818 or Thr840 enhances weighted mean channel conductance without altering response time course agonist potency. These data support idea these constitute a hyper-regulatory domain for receptor. Introduction phosphomimetic mutations increases only at three sites proximal terminus, consistent with structural model flexible linker connecting distal C-terminal to more containing helix bracketed Ser831 and Thr840. NMR spectra this raise possibility alter configuration domain. Our findings provide insight into structure function GluA1, which controls trafficking during synaptic plasticity in central nervous system.