Premium
Phosphorylation of Serine‐880 in GluR2 by Protein Kinase C Prevents Its C Terminus from Binding with Glutamate Receptor‐Interacting Protein
Author(s) -
Matsuda Shinji,
Mikawa Sumiko,
Hirai Hirokazu
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.731765.x
Subject(s) - ampa receptor , phosphorylation , glutamate receptor , microbiology and biotechnology , metabotropic glutamate receptor 6 , protein phosphorylation , synaptic plasticity , chemistry , pdz domain , protein kinase c , biology , biochemistry , protein kinase a , receptor
: Phosphorylation of the glutamate receptor is an important mechanism of synaptic plasticity. Here, we show that the C terminus of GluR2 of the α‐amino‐3‐hydroxy‐5‐methylisoxazole‐4‐propionate (AMPA) receptor is phosphorylated by protein kinase C and that serine‐880 is the major phosphorylation site. This phosphorylation also occurs in human embryonic kidney (HEK) cells by addition of 12‐ O ‐tetradecanoylphorbol 13‐acetate. Our immunoprecipitation experiment revealed that the phosphorylation of serine‐880 in GluR2 drastically reduced the affinity for glutamate receptor‐interacting protein (GRIP), a synaptic PDZ domain‐containing protein, in vitro and in HEK cells. This result suggests that modulation of serine‐880 phosphorylation in GluR2 controls the clustering of AMPA receptors at excitatory synapses and consequently contributes to synaptic plasticity.