Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-kappaB activation. Mol Cell Biol 2007 Jul;27(14):5235-45
Date
05/16/2007Pubmed ID
17502353Pubmed Central ID
PMC1951946DOI
10.1128/MCB.01645-06Scopus ID
2-s2.0-34447503930 (requires institutional sign-in at Scopus site) 33 CitationsAbstract
Bcl10 (B-cell lymphoma 10) is an adaptor protein comprised of an N-terminal caspase recruitment domain and a C-terminal serine/threonine-rich domain. Bcl10 plays a critical role in antigen receptor-mediated NF-kappaB 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-kappaB 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-kappaB activation.
Author List
Zeng H, Di L, Fu G, Chen Y, Gao X, Xu L, Lin X, Wen RMESH terms used to index this publication - Major topics in bold
Adaptor Proteins, Signal TransducingAnimals
B-Cell CLL-Lymphoma 10 Protein
Down-Regulation
Humans
Interleukin-2
Jurkat Cells
Lymphocyte Activation
Mice
Models, Biological
NF-kappa B
Phosphorylation
Receptors, Antigen, T-Cell
Serine
Ubiquitin
