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https://hdl.handle.net/2440/7504
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DC Field | Value | Language |
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dc.contributor.author | Tangye, S. | - |
dc.contributor.author | Lazetic, S. | - |
dc.contributor.author | Woollatt, E. | - |
dc.contributor.author | Sutherland, G. | - |
dc.contributor.author | Lanier, L. | - |
dc.contributor.author | Phillips, J. | - |
dc.date.issued | 1999 | - |
dc.identifier.citation | Journal of Immunology, 1999; 162(12):6981-6985 | - |
dc.identifier.issn | 0022-1767 | - |
dc.identifier.issn | 1550-6606 | - |
dc.identifier.uri | http://hdl.handle.net/2440/7504 | - |
dc.description.abstract | The genetic defect in X-linked lymphoproliferative syndrome (XLP) is the Src homology 2 domain-containing protein SAP. SAP constitutively associates with the cell surface molecule, signaling lymphocytic activation molecule (SLAM), and competes with SH2-domain containing protein tyrosine phosphatase-2 (SHP-2) for recruitment to SLAM. SLAM exhibits homology with the mouse cell surface receptor 2B4. The human homologue of 2B4 has now been identified. It is recognized by the c1.7 mAb, a mAb capable of activating human NK cells. Human 2B4 became tyrosine phosphorylated following pervanadate-treatment of transfected cells and recruited SHP-2. SAP was also recruited to 2B4 in activated cells. Importantly, the 2B4-SAP interaction prevented the association between 2B4 and SHP-2. These results suggest that the phenotype of XLP may result from perturbed signaling not only through SLAM, but also other cell surface molecules that utilize SAP as a signaling adaptor protein. | - |
dc.description.statementofresponsibility | Stuart G. Tangye, Sasha Lazetic, Erica Woollatt, Grant R. Sutherland, Lewis L. Lanier, and Joseph H. Phillips | - |
dc.language.iso | en | - |
dc.source.uri | http://www.jimmunol.org/content/162/12/6981 | - |
dc.subject | Killer Cells, Natural | - |
dc.subject | Cells, Cultured | - |
dc.subject | Humans | - |
dc.subject | Intracellular Signaling Peptides and Proteins | - |
dc.subject | Carrier Proteins | - |
dc.subject | Membrane Glycoproteins | - |
dc.subject | Receptors, Immunologic | - |
dc.subject | Antigens, CD | - |
dc.subject | Antibodies, Monoclonal | - |
dc.subject | Cloning, Molecular | - |
dc.subject | Signal Transduction | - |
dc.subject | Enzyme Activation | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | src Homology Domains | - |
dc.subject | Phosphorylation | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | Protein Tyrosine Phosphatases | - |
dc.subject | Protein Tyrosine Phosphatase, Non-Receptor Type 6 | - |
dc.subject | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | - |
dc.subject | SH2 Domain-Containing Protein Tyrosine Phosphatases | - |
dc.subject | Protein Phosphatase 2 | - |
dc.subject | Signaling Lymphocytic Activation Molecule Family | - |
dc.subject | Signaling Lymphocytic Activation Molecule Associated Protein | - |
dc.title | Cutting edge: Human 2B4, an activating NK cell receptor, recruits the protein tyrosine phosphatase SHP-2 and the adaptor signaling protein SAP | - |
dc.type | Journal article | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest Paediatrics publications |
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