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Beschreibung

The NK cell receptor protein 1 (NKR-P1), a.k.a. CD161, molecules represent a family of type II transmembrane C-type lectin-like receptors expressed predominantly by NK cells. A total of five murine NKR-P1-coding genes (Klrb1a/b/c/d/f) have been identified, with NKR-P1A/C/F (CD161a/c/f) functioning as stimulatory receptors that possess a charged transmembrane arginine esidue thought to be important for association with the FcRgamma adaptor protein, and NKR-P1B/D as two inhibitory receptors that possess a consensus cytoplasmic ITIM (L/VxYxxL/I/V) motif. The ITIM motif is shown to mediate NKR-P1B recruitment of Src homology 2 (SH2)-containing protein tyrosine phosphatase-1 (SHP-1) in a phosphorylation-dependent manner. All murine NKR-P1 proteins possess a Cys-X-Cys-Pro (CxCP) motif that mediates association with the Src-related nonreceptor protein tyrosine kinase p56lck. Both NKR-P1B and NKR-P1C functionally associate with p56lck, while mutation of the CxCP motif abolishes NKR-P1B/C-mediated signal transduction. Likewise, mutation of ITIM motif abolishes NKR-P1B SHP-1 association as well as NKR-P1B-dependent inhibitory signaling.

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