Abstract
Bcl10 (B-cell lymphoma 10) is an adaptor protein comprised of an N-tenninal caspase recruitment domain and a C-terminal serine/threonine-rich domain. Bcl10 plays a critical role in antigen receptor-mediated NF-κB activation and lymphocyte development and functions. Our current study has discovered that T-cell activation induced monophosphorylation and biphosphorylation of Bcl10 and has identified S138 within Bcl10 as one of the T-cell receptor-induced phosphorylation sites. Alteration of S138 to an alanine residue impaired T-cell activation-induced ubiquitination and subsequent degradation of Bcl10, ultimately resulting in prolongation of TCR-mediated NF-κB activation and enhancement of interleukin-2 production. Taken together, our findings demonstrate that phosphorylation of Bcl10 at S138 down-regulates Bcl10 protein levels and thus negatively regulates T-cell receptor-mediated NF-κB activation.
Original language | English (US) |
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Pages (from-to) | 5235-5245 |
Number of pages | 11 |
Journal | Molecular and cellular biology |
Volume | 27 |
Issue number | 14 |
DOIs | |
State | Published - Jul 2007 |
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology