Abstract
Natural killer (NK) cells express killer inhibitory receptors that mediate negative regulation of NK cell cytotoxicity upon binding to MHC class I molecules on target cells. Unrelated inhibitory receptors on B cells have recently been shown to function through recruitment of phosphotyrosine phosphatase 1C (PTP-1C). Here, we show that a human killer inhibitory receptor specific for HLA-C also recruits PTP-1C after phosphorylation induced either by the pharmacological agent phenylarsine oxide or by conjugation with target cells. This recruitment is mediated by the binding of specific cytoplasmic phosphotyrosine-containing sequences to PTP-1C. These results implicate PTP-1C as a cytosolic component of the negative signaling pathway through NK cell inhibitory receptors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Calcium / physiology
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Clone Cells
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Cytotoxicity, Immunologic
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Enzyme Activation
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HLA-C Antigens / metabolism
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Humans
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Intracellular Signaling Peptides and Proteins
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Killer Cells, Natural / physiology*
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Molecular Sequence Data
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Peptides / chemistry
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Phosphorylation
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Phosphotyrosine / metabolism*
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases / metabolism*
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Receptors, Immunologic / metabolism*
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Signal Transduction
Substances
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HLA-C Antigens
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Intracellular Signaling Peptides and Proteins
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Peptides
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Receptors, Immunologic
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Phosphotyrosine
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PTPN11 protein, human
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PTPN6 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases
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Calcium