Journal
JOURNAL OF IMMUNOLOGY
Volume 190, Issue 6, Pages 2924-2930Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1201032
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Funding
- Wellcome Trust
- Medical Research Council, United Kingdom
- BBSRC [BB/I013407/2] Funding Source: UKRI
- MRC [G1001044, G1001738, G0500563] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I013407/2] Funding Source: researchfish
- Medical Research Council [G0500563, G1001738, G1001044] Funding Source: researchfish
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Productive engagement of MHC class I by inhibitory NK cell receptors depends on the peptide bound by the MHC class I molecule. Peptide: MHC complexes that bind weakly to killer cell Ig-like receptors (KIRs) can antagonize the inhibition mediated by high-affinity peptide: MHC complexes and cause NK cell activation. We show that low-affinity peptide: MHC complexes stall inhibitory signaling at the step of Src homology protein tyrosine phosphatase 1 recruitment and do not go on to form the KIR microclusters induced by high-affinity peptide: MHC, which are associated with Vav dephosphorylation and downstream signaling. Furthermore, the low-affinity peptide: MHC complexes prevented the formation of KIR microclusters by high-affinity peptide: MHC. Thus, peptide antagonism of NK cells is an active phenomenon of inhibitory synapse disruption. The Journal of Immunology, 2013, 190: 2924-2930.
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