An activating immunoreceptor complex formed by NKG2D and DAP10.
Many immune receptors are composed of separate ligand-binding and signal-transducing subunits. In natural killer (NK) and T cells, DAP10 was identified as a cell surface adaptor protein in an activating receptor complex with NKG2D, a receptor for the stress-inducible and tumor-associated major histocompatibility complex molecule MICA. Within the DAP10 cytoplasmic domain, an Src homology 2 (SH2) domain-binding site was capable of recruiting the p85 subunit of the phosphatidylinositol 3-kinase (PI 3-kinase), providing for NKG2D-dependent signal transduction. Thus, NKG2D-DAP10 receptor complexes may activate NK and T cell responses against MICA-bearing tumors.
Pubmed ID: 10426994 RIS Download
Amino Acid Sequence | Animals | Binding Sites | Cell Line | Cytotoxicity, Immunologic | Humans | Killer Cells, Natural | Ligands | Lymphocyte Activation | Membrane Proteins | Mice | Molecular Sequence Data | NK Cell Lectin-Like Receptor Subfamily K | Neoplasms | Phosphatidylinositol 3-Kinases | Phosphorylation | Phosphotyrosine | Receptors, Immunologic | Receptors, Natural Killer Cell | Signal Transduction | T-Lymphocytes | Tumor Cells, Cultured | src Homology Domains