Phosphoproteomic analyses reveal that galectin-1 augments the dynamics of B-cell receptor signaling.

摘要: Abstract B-cell activation is important for mounting humoral immune responses and antibody production. Galectin-1 has multiple regulatory functions in cells. However, the effects of galectin-1 modulation mechanisms underlying coordination are unclear. To address this issue, we applied label-free quantitative phosphoproteomic analysis to investigate dynamics galectin-1-induced signaling comparison with that following anti-IgM treatment. A total 3247 phosphorylation sites on 1245 proteins were quantified, 70–80% 856 responsive phosphoproteins commonly activated during various biological functions. The similarity between galectin-1- anti-IgM-elicited receptor (BCR) pathways was also revealed. Additionally, mapping 149 BCR-responsive provided complementary knowledge BCR signaling. Compared induction, profiling signaling, along validation by western blot pharmacological inhibitors, revealed Syk, Btk, PI3K may be dominant galectin-1-mediated activation. We further demonstrated proliferation antigen-primed B cells diminished absence an animal model. Together, these findings evidence a new role insight into mechanism how augments strength immunological synapse modulating Biological significance current study first systematic phosphorylation-mediated network its cell comparative induced profiles not only showed exogenously added augmented but relatively enhanced pathway. Together assay, delineated response antigen challenge. Our reveals augmenting