细胞生物学
磷酸化
BCL10
离子霉素
生物
T细胞受体
肌动蛋白
Jurkat细胞
化学
T细胞
免疫系统
生物化学
免疫学
细胞内
基因
作者
Daniel Rueda,Olivier Gaide,Liza Ho,Elodie Lewkowicz,Florence Niedergang,Stephan Hailfinger,Fabien Rebeaud,Montserrat Guzzardi,Béatrice Conne,Marcus Thelen,Jérôme Delon,Uta Ferch,Tak W. Mak,Jürgen Ruland,Juerg Schwaller,Margot Thome
出处
期刊:Journal of Immunology
[American Association of Immunologists]
日期:2007-04-01
卷期号:178 (7): 4373-4384
被引量:44
标识
DOI:10.4049/jimmunol.178.7.4373
摘要
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.
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