Engagement of cell-surface receptors leads to activation of protein tyrosine kinases, which in turn phosphorylate various downstream enzymes and adaptor proteins. Lnk is an adaptor protein that appears to be involved in signal transduction in lymphocytes, and forms an adaptor protein family with SH2-B. We tried to identify another member of the adaptor protein family and isolated the mouse APS (adaptor molecule containing PH and SH2 domains). APS contains a proline-rich region, PH and SH2 domains, and a putative tyrosine phosphorylation site at the C-terminal, and the overall structure resembles those of Lnk and SH2-B. APS is expressed in brain, kidney, muscle, and mature B cells in spleen. Mouse APS gene consists of 8 coding exons and is deduced to map to chromosome 5. APS is tyrosine phosphorylated at the C-terminal phosphorylation site conserved among the Lnk family adaptor proteins by stimulation of IL-5 or IL-3 as well as by crosslinking of B cell receptor complex. These results suggest that APS is a member of the Lnk family adaptor protein and likely plays a role in signaling in B cells.
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