Interaction of GPI-anchored cell surface proteins and complement receptor type 3.
Glycosylphosphatidylinositol (GPI)-anchored cell surface proteins lack transmembrane and cytoplasmic domains. For some of them, such as CD14, CD16b and CD87, it could be demonstrated recently that they are physically and functionally associated with complement receptor type 3 (CR3, CD11b/CD18). Also, there are indications that in certain cells these GPI proteins employ CR3 as an adapter for signal transduction across the plasma membrane.
Stockinger
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Institute of Immunology-VIRCC, University of Vienna, Austria. Johannes.Stockinger@univie.ac.at
D015703:Antigens, CD / Q000378:metabolism; D002462:Cell Membrane / Q000276:immunology / Q000378:metabolism; D017261:Glycosylphosphatidylinositols / Q000378:metabolism*; D006801:Humans; D016177:Macrophage-1 Antigen / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D015398:Signal Transduction
D015703:Antigens, CD; D017261:Glycosylphosphatidylinositols; D016177:Macrophage-1 Antigen; D008565:Membrane Proteins; D011505:Protein-Tyrosine Kinases