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/CXCR2,2 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. (C) 2008 Elsevier B.V. All rights reserved.
Chemokine CXCL8 modulates GluR1 phosphorylation / Catalano, Myriam; Trettel, Flavia; Cipriani, Raffaela; Lauro, Clotilde; Fabrizia, Sobrero; Eusebi, Fabrizio; Limatola, Cristina. - In: JOURNAL OF NEUROIMMUNOLOGY. - ISSN 0165-5728. - STAMPA. - 198:1-2(2008), pp. 75-81. [10.1016/j.jneuroim.2008.04.017]