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Overview
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Background
CD79a (Ig α, MB1) forms disulfide-linked heterodimer with CD79b (Ig β, B29). They both are transmembrane proteins with extended cytoplasmic domains containing immunoreceptor tyrosine activation motives (ITAMs), and together with cell surface immunoglobulin they constitute B-cell antigen-specific receptor (BCR). CD79a and b are the first components of BCR that are expressed developmentally. They appear on pro-B cells in association with the endoplasmic reticulum chaperone calnexin. Subsequently, in pre-B cells, CD79 heterodimer is associated with λ5-VpreB surrogate immunoglobulin and later with antigen-specific surface immunoglobulins. At the plasma cell stage, CD79a is present as an intracellular component. CD79a/b complex interacts with Src-family tyrosine kinase Lyn, which phosphorylates its cytoplasmic ITAM motives to form docking sites for downstream signaling.
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