Amy Reichlin

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The B cell receptor (BCR) regulates B cell development and function through immunoglobulin (Ig)alpha and Ig beta, a pair of membrane-bound Ig superfamily proteins, each of which contains a single cytoplasmic immunoreceptor tyrosine activation motif (ITAM). To determine the function of Ig beta, we produced mice that carry a deletion of the cytoplasmic domain(More)
To determine the function of immunoglobulin (Ig) ␣ immunoreceptor tyrosine–based activation motif (ITAM) phosphorylation, we generated mice in which Ig ␣ ITAM tyrosines were replaced by phenylalanines (Ig ␣ FF/FF). Ig ␣ FF/FF mice had a specific reduction of B1 and marginal zone B cells, whereas B2 cell development appeared to be normal, except that ␭ 1(More)
Immunoglobulin (Ig)alpha and Igbeta initiate B cell receptor (BCR) signaling through immune receptor tyrosine activation motifs (ITAMs) that are targets of SH2 domain-containing kinases. To examine the function of Igbeta ITAM tyrosine resides in mature B cells in vivo, we exchanged these residues for alanine by gene targeting (Igbeta(AA)). Mutant mice(More)
B cell receptor (BCR) signaling is mediated through immunoglobulin (Ig)alpha and Igbeta a membrane-bound heterodimer. Igalpha and Igbeta are redundant in their ability to support early B cell development, but their roles in mature B cells have not been defined. To examine the function of Igalpha-Igbeta in mature B cells in vivo we exchanged the cytoplasmic(More)
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