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The cell surface receptor CD6 regulates T cell activation in both activating and inhibitory manners. The adaptor protein SLP-76 is recruited to the phosphorylated CD6 cytoplasmic Y662 residue during T cell activation, providing an activating signal to T cells. In this study, a biochemical approach identified the SH2 domain-containing adaptor protein GADS as the dominant interaction partner for the CD6 cytoplasmic Y629 residue. Functional experiments in human Jurkat and primary T cells showed that both mutations Y629F and Y662F abolished costimulation by CD6. In addition, a restraint on T cell activation by CD6 was revealed in primary T cells expressing CD6 mutated at Y629 and Y662. These data are consistent with a model in which bivalent recruitment of a GADS/SLP-76 complex is required for costimulation by CD6.

Original publication




Journal article


Mol Cell Biol

Publication Date





CD6, GADS, SLP-76, T cells, signal transduction, Adaptor Proteins, Signal Transducing, Antigens, CD, Antigens, Differentiation, T-Lymphocyte, CD4-Positive T-Lymphocytes, Humans, Interleukin-2, Jurkat Cells, Lymphocyte Activation, Models, Biological, Mutant Proteins, Mutation, Phosphoproteins, Protein Binding, T-Lymphocytes, src Homology Domains