Journal
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
Volume 54, Issue -, Pages 217-222Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2014.07.012
Keywords
NF-kappa B; Lymphocytes; Ubiquitylation; Signaling
Categories
Funding
- French National Research Agency [ANR-10-JCJC-1306]
- Fondation ARC
- Fondation ARC, Ligue Nationale contre le Cancer
- Fondation pour la Recherche Medicale
- Institut National du Cancer [INCA_6508]
- Ligue Nationale contre le Cancer
- Agence Nationale de la Recherche (ANR) [ANR-10-JCJC-1306] Funding Source: Agence Nationale de la Recherche (ANR)
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The nuclear factor kappa B (NF-kappa B) family members p65 and c-Rel chiefly orchestrate lymphocytes activation following T-cell receptor (TCR) engagement. In contrast to p65, which is rapidly mobilized, c-Rel activation occurs subsequently as it involves a nuclear factor of activated T-cells (NFAT)-dependent upregulation step. However, how TCR ligation drives p65 and c-Rel activation is not fully understood. Because several ubiquitylated components of NF-kappa B signaling cascade accumulate in close proximity to membranes, we screened a siRNA library against E3-ligases that contain transmembrane domains on TCR-mediated NF-kappa B activation. Here, we report the identification of the endoplasmic reticulum resident TRIM 13 protein as an enhancer of NF-kappa B promoter activity. We found that knocking down TRIM13 by RNA interference reduced the activation of p65, while the translocation of c-Rel into the nucleus was blunted. We further observed that c-Rel induction was diminished without TRIM13, as NFAT activation was compromised. These results unveil that TRIM13 is a selective regulator of p65 and of c-Rel activation. (C) 2014 Elsevier Ltd. All rights reserved.
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