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- Publisher Website: 10.4049/jimmunol.178.7.4373
- Scopus: eid_2-s2.0-33947707994
- PMID: 17371994
- WOS: WOS:000245197300044
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Article: Bcl10 controls TCR- and FCγR-induced actin polymerization
Title | Bcl10 controls TCR- and FCγR-induced actin polymerization |
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Authors | |
Issue Date | 2007 |
Citation | Journal of Immunology, 2007, v. 178, n. 7, p. 4373-4384 How to Cite? |
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. Copyright © 2007 by The American Association of Immunologists, Inc. |
Persistent Identifier | http://hdl.handle.net/10722/292598 |
ISSN | 2023 Impact Factor: 3.6 2023 SCImago Journal Rankings: 1.558 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Rueda, Daniel | - |
dc.contributor.author | Gaide, Olivier | - |
dc.contributor.author | Ho, Liza | - |
dc.contributor.author | Lewkowicz, Elodie | - |
dc.contributor.author | Niedergang, Florence | - |
dc.contributor.author | Hailfinger, Stephan | - |
dc.contributor.author | Rebeaud, Fabien | - |
dc.contributor.author | Guzzardi, Montserrat | - |
dc.contributor.author | Conne, Béatrice | - |
dc.contributor.author | Thelen, Marcus | - |
dc.contributor.author | Delon, Jérôme | - |
dc.contributor.author | Ferch, Uta | - |
dc.contributor.author | Mak, Tak W. | - |
dc.contributor.author | Ruland, Jürgen | - |
dc.contributor.author | Schwaller, Jürg | - |
dc.contributor.author | Thome, Margot | - |
dc.date.accessioned | 2020-11-17T14:56:49Z | - |
dc.date.available | 2020-11-17T14:56:49Z | - |
dc.date.issued | 2007 | - |
dc.identifier.citation | Journal of Immunology, 2007, v. 178, n. 7, p. 4373-4384 | - |
dc.identifier.issn | 0022-1767 | - |
dc.identifier.uri | http://hdl.handle.net/10722/292598 | - |
dc.description.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. Copyright © 2007 by The American Association of Immunologists, Inc. | - |
dc.language | eng | - |
dc.relation.ispartof | Journal of Immunology | - |
dc.title | Bcl10 controls TCR- and FCγR-induced actin polymerization | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.4049/jimmunol.178.7.4373 | - |
dc.identifier.pmid | 17371994 | - |
dc.identifier.scopus | eid_2-s2.0-33947707994 | - |
dc.identifier.volume | 178 | - |
dc.identifier.issue | 7 | - |
dc.identifier.spage | 4373 | - |
dc.identifier.epage | 4384 | - |
dc.identifier.isi | WOS:000245197300044 | - |
dc.identifier.issnl | 0022-1767 | - |