| First Author | Su YW | Year | 1999 |
| Journal | Eur J Immunol | Volume | 29 |
| Issue | 11 | Pages | 3702-11 |
| PubMed ID | 10556826 | Mgi Jnum | J:243546 |
| Mgi Id | MGI:5908798 | Doi | 10.1002/(SICI)1521-4141(199911)29:11<3702::AID-IMMU3702>3.0.CO;2-R |
| Citation | Su YW, et al. (1999) Interaction of SLP adaptors with the SH2 domain of Tec family kinases. Eur J Immunol 29(11):3702-11 |
| abstractText | 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. |
