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	Eur. J. Immunol. Nov (1999); 29(11):3702-11
Interaction of SLP adaptors with the SH2 domain of Tec family kinases.
Su YW, Zhang Y, Schweikert J, Koretzky GA, Reth M, Wienands J
Abteilung fur Molekulare Immunologie Biologie III, Universitat Freiburg und Max-Planck-Institut fur Immunbiologie, Freiburg, Germany.
Abstract: Activation of lymphocytes through their antigen receptors leads to mobilization of intracellular Ca(2+) ions. This process requires expression of SLP adaptors and involves phosphorylation of phospholipase C-gamma isoforms by the Tec-related protein tyrosine kinase Btk in B cells and Itk in T cells. The SH2 domain of Btk and Itk is essential for phospholipase C-gamma phosphorylation and mutations in this domain lead to the X-linked agammaglobulinemia immuno deficiency in humans. Here we show that, in contrast to SH2 domains from other signaling proteins, the Btk and Itk SH2 domains exhibit a restricted binding specificity. They bind selectively to tyrosine-phosphorylated SLP-65 and SLP-76 in activated B and T cells, respectively. Our findings suggest that Btk/Itk and phospholipase C-gamma both bind via their SH2 domain to phosphorylated SLP adaptors, and that this association is required for the activation of phospholipase C-gamma.
[PUBMED: 10556826]