Details

Autor(en) / Beteiligte

• Rueda, Daniel
• Gaide, Olivier
• Ho, Liza
• Lewkowicz, Elodie
• Niedergang, Florence
• Hailfinger, Stephan
• Rebeaud, Fabien
• Guzzardi, Montserrat
• Conne, Béatrice
• Thelen, Marcus
• Delon, Jérôme
• Ferch, Uta
• Mak, Tak W.
• Ruland, Jürgen
• Schwaller, Jürg
• Thome, Margot

Titel

Bcl10 Controls TCR- and FcγR-Induced Actin Polymerization

Ist Teil von

• Journal of Immunology, 2007-04, Vol.178 (7), p.4373-4384

Erscheinungsjahr

2007

Quelle

Wiley Online Library - AutoHoldings Journals

Beschreibungen/Notizen

• Abstract Bcl10 plays an essential role in the adaptive immune response, because Bcl10-deficient lymphocytes show impaired Ag receptor-induced NF-κB activation and cytokine production. Bcl10 is a phosphoprotein, but the physiological relevance of this posttranslational modification remains poorly defined. In this study, we report that Bcl10 is rapidly phosphorylated upon activation of human T cells by PMA/ionomycin- or anti-CD3 treatment, and identify Ser138 as a key residue necessary for Bcl10 phosphorylation. We also show that a phosphorylation-deficient Ser138/Ala mutant specifically inhibits TCR-induced actin polymerization yet does not affect NF-κB activation. Moreover, silencing of Bcl10, but not of caspase recruitment domain-containing MAGUK protein-1 (Carma1) induces a clear defect in TCR-induced F-actin formation, cell spreading, and conjugate formation. Remarkably, Bcl10 silencing also impairs FcγR-induced actin polymerization and phagocytosis in human monocytes. These results point to a key role of Bcl10 in F-actin-dependent immune responses of T cells and monocytes/macrophages.