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Fc receptor-like protein 2 is a transmembrane glycoprotein member of the immunoglobulin receptor superfamily, predominantly expressed on human B cells, especially memory B cells. It contains four extracellular C2-type immunoglobulin domains, a transmembrane region, and a cytoplasmic domain with one immunoreceptor-tyrosine activation motif (ITAM-like) and two immunoreceptor-tyrosine inhibitory motifs (ITIMs). Upon activation, the ITIMs recruit the tyrosine phosphatase SHP-1, thereby inhibiting B cell receptor-mediated signal transduction. This regulatory function positions FCRL2 as a negative modulator of B cell activation and as a biomarker for less aggressive, mutated forms of chronic lymphocytic leukemia. The endogenous ligand for FCRL2 remains unknown, and its expression is largely restricted to lymphoid tissues such as spleen, lymph node, and tonsil, as well as peripheral blood B cells[1][2][3].
Inhibition of B cell receptor (BCR) signaling via recruitment of SHP-1 phosphatase to ITIM motifs, Immunomodulatory effects on B lymphocyte activation
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