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Abstract Ly-49D is an activating receptor on NK cells that does not become tyrosine phosphorylated upon activation. This report demonstrates that immunoprecipitation of Ly-49D, following pervanadate treatment or specific Ab cross-linking, coprecipitates a 16-kDa tyrosine-phosphorylated protein (pp16). Immunoblotting experiments and data from TCR-ζ/FcεRIγ double knockout mice confirm that pp16 is not TCR-ζ, TCR-η, or FcεRIγ. Association of pp16 with Ly-49D involves a transmembrane arginine since mutation to leucine (Ly-49DR54L) abolishes association with pp16 in transfected P815 cells. In addition, Ly-49DR54L transfectants fail to mediate Ca2+ mobilization following Ab cross-linking. Therefore, signaling through Ly-49D on NK cells depends on association with a distinct tyrosine phosphoprotein (pp16) in a manner analogous to that of TCR and FcR. Expression of this novel signaling peptide in both the NK and myeloid lineages indicates that pp16 is likely involved in the signal transduction cascade of additional receptor families.
Mason et al. (Fri,) studied this question.
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