The B cell receptor promotes B cell activation and proliferation through a non-ITAM tyrosine in the Ig alpha cytoplasmic domain

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In addition to the tyrosines of the Ig alpha and beta immunoreceptor tyrosine-based activation motifs (ITAMs), the evolutionarily conserved Ig alpha non-ITAM tyrosine 204 becomes phosphorylated upon antigen recognition by the B cell receptor (BCR). Here we demonstrate that splenic B cells from mice with a targeted mutation of Ig alpha Y204 exhibited an isolated defect in T cell-independent B cell activation, proliferation, and antibody response upon BCR engagement, yet normal BCR capping, antigen internalization, antigen presentation, and T cell-dependent antibody production. Mutant B cells, present in normal numbers, exhibited unimpaired BCR-induced spleen tyrosine kinase (Syk) phosphorylation but reduced B cell linker protein (BLNK) phosphorylation, calcium flux, and nuclear factor kappa B (NF kappa B), c-jun N-terminal kinase (JNK), and extracellular signal-regulated kinase (ERK) activation. These results suggest that Ig alpha non-ITAM tyrosine 204 promotes a distinct cellular response, namely T-independent B cell proliferation and differentiation via phosphorylation of the adaptor BLNK.
Publisher
CELL PRESS
Issue Date
2006-07
Language
English
Article Type
Article
Keywords

ANTIGEN RECEPTOR; LINKER PROTEIN; MOTIF ITAM; KAPPA-B; BLNK; LYMPHOCYTES; MICE; SLP-65; SYK; PHOSPHORYLATION

Citation

IMMUNITY, v.25, no.1, pp.55 - 65

ISSN
1074-7613
DOI
10.1016/j.immuni.2006.04.014
URI
http://hdl.handle.net/10203/240859
Appears in Collection
MSE-Journal Papers(저널논문)
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