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Tyrosine phosphorylation of a human killer inhibitory receptor recruits protein tyrosine phosphatase 1C.
- Source :
-
The Journal of experimental medicine [J Exp Med] 1996 Jul 01; Vol. 184 (1), pp. 93-100. - Publication Year :
- 1996
-
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.
- Subjects :
- Amino Acid Sequence
Calcium physiology
Clone Cells
Cytotoxicity, Immunologic
Enzyme Activation
HLA-C Antigens metabolism
Humans
Intracellular Signaling Peptides and Proteins
Molecular Sequence Data
Peptides chemistry
Phosphorylation
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Signal Transduction
Killer Cells, Natural physiology
Phosphotyrosine metabolism
Protein Tyrosine Phosphatases metabolism
Receptors, Immunologic metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1007
- Volume :
- 184
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- The Journal of experimental medicine
- Publication Type :
- Academic Journal
- Accession number :
- 8691154
- Full Text :
- https://doi.org/10.1084/jem.184.1.93