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The serine and threonine residues in the Ig-a cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction



The serine and threonine residues in the Ig-a cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction



Proceedings of the National Academy of Sciences of the United States of America 97(15): 51-4



Regulation of signal transduction from the B cell antigen receptor (BCR) was investigated. The BCR is a multiprotein complex that consists of the membrane-bound immunoglobulin (Ig) molecule and the Ig-a/Igb heterodimer; on BCR engagement, Ig-a and Ig-b become phosphorylated on tyrosine residues of the immunoreceptor tryosine-based activation motif (ITAM) as well as on serine and threonine residues. Mutation of all 3 serine and threonine residues in the Ig-a cytoplasmic portion revealed that they negatively regulate phosphorylation of the ITAM tyrosines.

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