Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-κB activation

Hu Zeng, Lie Di, Guoping Fu, Yuhong Chen, Xiang Gao, Langlai Xu, Xin Lin, Renren Wen

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


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 languageEnglish (US)
Pages (from-to)5235-5245
Number of pages11
JournalMolecular and cellular biology
Issue number14
StatePublished - Jul 2007

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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