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Abstract

Signal transduction by the B cell antigen receptor (BCR) regulates development, survival and clonal expansion of B cells. The BCR complex comprises the membrane-bound immunoglobulin molecule (mlg) and the Ig-α/Ig-β heterodimer, and was shown to form oligomeric structures. In pervanadate (PV)-treated B cells, multiple proteins are tyrosine phosphorylated upon expression of the BCR, indicating that the BCR can signal in an antigen-independent fashion. We analyzed the signal transduction from BCR mutants which either have an altered heavy chain transmembrane region or lack the Ig-α cytoplasmic tail. In comparison to cells expressing the wild-type receptors, those with a mutant BCR respond to PV treatment with reduced and retarded tyrosine phosphorylation of substrate proteins. Conversely, the cells with mutant BCR are more sensitive to stimulation with low doses of antigen. These data suggest that a correctly assembled BCR complex is important for antigen-independent Signaling and setting the threshold for antigen-dependent BCR activation.