Chemokine CXCL8 modulates GluR1 phosphorylation

被引：10

作者：

Catalano, Myniam ^{[2
,3
]}

Trettel, Flavia ^{[2
,3
]}

Cipriani, Raffaela ^{[2
,3
]}

Lauro, Clotilde ^{[2
,3
]}

Sobrero, Fabrizia ^{[2
,3
]}

Eusebi, Fabrizio ^{[1
]}

Limatola, Cristina ^{[1
]}

机构：

[1] Neuromed Ist Ricovero & Cura Carattere Seci, I-86077 Isernia, Italy

[2] Univ Roma La Sapienza, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy

[3] Univ Roma La Sapienza, Ctr Eccellenza BEMM, Dipartimento Fisiol Umana & Farmacol, I-00185 Rome, Italy

来源：

JOURNAL OF NEUROIMMUNOLOGY | 2008年 / 198卷 / 1-2期

关键词：

CXCL8; phosphorylation; glutamate receptor; chemotaxis;

D O I：

10.1016/j.jneuroim.2008.04.017

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

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.

引用

页码：75 / 81

页数：7

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