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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


  • Wu J
  • Song Y
  • Bakker AB
  • Bauer S
  • Spies T
  • Lanier LL
  • Phillips JH


Science (New York, N.Y.)

Publication Data

July 30, 1999

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI30581

Mesh Terms

  • 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