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The Journal of Immunology, Vol 156, Issue 12 4531-4534, Copyright © 1996 by American Association of Immunologists
CUTTING EDGE |
L Olcese, P Lang, F Vely, A Cambiaggi, D Marguet, M Blery, KL Hippen, R Biassoni, A Moretta, L Moretta, JC Cambier and E Vivier
Center for Immunology, INSERM/CNRS of Marseille-Luminy, France.
NK cells express cell surface receptors for MHC class I proteins (KIR). Engagement of these receptors inhibits NK cell cytotoxic programs. KIR can be expressed on T cells, and their engagement also results in inhibition of effector functions initiated by the CD3/TCR complex. While human KIR genes belong to the Ig gene superfamily, mouse KIR belong to a family of dimeric lectins. Despite these distinct evolutionary origins, we show here that both HLA-Cw3-specific human p58.183 receptors and H-2D d/k-specific mouse Ly49A receptors recruit the same protein tyrosine phosphatases, PTP1C and PTP1D, upon phosphorylation of critical intracytoplasmic tyrosine residues. These results document a common pathway by which diverse KIR can down- regulate NK and T cell activation programs, and further define the sequence of the immunoreceptor tyrosine-based inhibitory motif (ITIM), initially described in FcgammaRIIB1, and expressed in both human and mouse KIR.
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