Back to Search
Start Over
TRIM13 regulates ubiquitination and turnover of NEMO to suppress TNF induced NF-κB activation.
- Source :
-
Cellular Signalling . Dec2014, Vol. 26 Issue 12, p2606-2613. 8p. - Publication Year :
- 2014
-
Abstract
- The NF-κB family of transcription factors is activated in response to various intracellular or extracellular stimuli and its dysregulation leads to pathological conditions like infection, cancer, neurodegenerative disorders. The post-translational modification by ubiquitination regulates various steps of NF-κB pathway. In the current study, we have described the role of TRIM13, an endoplasmic reticulum (ER) membrane anchored E3 ligase in regulation of NF-κB. The expression of TRIM13 represses TNF induced NF-κB while the knockdown has the opposite effect. The E3 ligase activity and ER localization is essential for NF-κB suppression whereas TRIM13 regulated autophagy is not essential. TRIM13 interacts with NEMO and modulates its ubiquitination and turnover, hence may regulate IKK complex activity. TRIM13 mediated NF-κB repression is essential for negative regulation of clonogenic ability of the cells. This study for the first time demonstrated the role of TRIM13, ER resident RING E3 ligase as a novel regulator of NEMO ubiquitination, negative regulator of NF-κB signaling and its role as a tumor suppressor. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 08986568
- Volume :
- 26
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Cellular Signalling
- Publication Type :
- Academic Journal
- Accession number :
- 99105714
- Full Text :
- https://doi.org/10.1016/j.cellsig.2014.08.008