Selective cross-talk among natural cytotoxicity receptors in XXXX natural killer cells.

@entity1 @entity9707 @entity3222 @entity5 @entity12711 @entity9656 @entity9706 @entity4071 @entity32883 @entity669 @entity3221 @entity19124
The cytolytic activity of @entity1 natural killer cells is induced by several triggering cell surface receptors upon interaction with specific cellular ligands. These receptors include @entity3222 , @entity3221 and @entity19124 , collectively termed natural cytotoxicity receptors (NCR). Co-operation among NCR has been shown to occur for optimal recognition and killing of most @entity5 target cells. In this study, we show that the mAb-mediated engagement and clustering of one or another NCR results in the activation of an identical set of @entity669 kinases. These kinases are included in the signaling cascade leading to @entity669 phosphorylation of different receptor-associated signal transducing molecules i.e. @entity12711 (associated with @entity3222 and @entity3221 ) and @entity9656 / @entity9656 (associated with @entity19124 ). In line with the notion that the engagement of inhibitory receptors prevents NCR-mediated responses, we show that the engagement of @entity9706 / @entity9707 virtually abrogates the @entity669 phosphorylation of the NCR-associated signaling molecules, i.e. it acts at the very early steps of the signaling cascade. Importantly, the engagement of a single NCR resulted in the activation of the signaling cascades associated with the other NCR. This "cross-talk" is confined to @entity3222 , @entity3221 and @entity19124 since neither @entity4071 -nor @entity32883 -associated signaling polypeptides were phosphorylated following the NCR engagement. These results suggest that a functional cross-talk specifically occurs among different NCR, possibly resulting in the amplification of the activating signals.
