Chemokine CXCL8 modulates GluR1 phosphorylation.

The chemokine interleukin 8/CXCL8 induces the phosphorylation of the GluR1 subunit of the AMPA-type glutamate receptor in neurons and transfected HEK cells, on both serine 845 (S845) and 831 (S831) residues. We previously described that CXCL8 receptor CXCR2 and GluR1 co-precipitate and that GluR1/CXCR2 co-expression both in HEK cells and ...
neurons impairs CXCL8-induced cell migration. Here we show that replacement of S845 with Ala (A), but not with Glu (E), strongly reduces GluR1/CXCR2 interaction and abolishes the impairment of CXCL8-induced cell migration. Considered together our findings point to the phosphorylated state of S845GluR1 as a determinant of GluR1-CXCR2 physical coupling.
Mesh Terms:
Animals, Animals, Newborn, Calcium, Carbazoles, Cells, Cultured, Cerebellum, Chelating Agents, Chemotaxis, Cyclic AMP, Egtazic Acid, Enzyme Inhibitors, Gene Expression Regulation, Hippocampus, Humans, Interleukin-8, Mutation, Neurons, Phosphorylation, Pyrroles, Rats, Rats, Sprague-Dawley, Receptors, AMPA, Time Factors, Transfection
J Neuroimmunol
Date: Jul. 31, 2008
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