Chemokine CXCL8 modulates GluR1 phosphorylation

Myriam Catalano, Flavia Trettel, Raffaela Cipriani, Clotilde Lauro, Fabrizia Sobrero, Fabrizio Eusebi, Cristina Limatola

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)75-81
Number of pages7
JournalJournal of Neuroimmunology
Issue number1-2
Publication statusPublished - Jul 31 2008


  • Chemotaxis
  • CXCL8
  • Glutamate receptor
  • Phosphorylation

ASJC Scopus subject areas

  • Immunology
  • Clinical Neurology
  • Immunology and Allergy
  • Neurology


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