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The human NKG2D ligand ULBP2 can be expressed at the cell surface with or without a GPI anchor and both forms can activate NK cells

AuthorsReyburn, H. T. ; Valés-Gómez, M.
KeywordsGPI-anchored proteins
Innate Immunity
ER trafficking
Issue DateFeb-2011
PublisherCompany of Biologists
CitationJournal of Cell Science 124: 321-32 (2011)
AbstractThe activating immune receptor NKG2D binds to multiple stress-induced ligands that are structurally different: MHC-class I-related Chain (MIC) A/B molecules have a transmembrane domain whereas most UL16 binding proteins (ULBPs) are glycosylphosphatidyl-inositol (GPI)-linked molecules. The significance of this variability in membrane anchor is unclear. Here, we demonstrate that ULBP2, but not ULBP1 or 3, can reach the cell surface without the GPI modification. Several proteins are expressed at the cell surface as both transmembrane and GPI-linked molecules, either via alternative splicing or by the expression of linked genes. However, to our knowledge, ULBP2 is the first single mammalian cDNA that can be expressed as either a transmembrane or a GPI-anchored protein. The rate of maturation and the levels of cell surface expression of the non-GPI linked form were lower than those of the GPI-linked ULBP2. Nonetheless, non-GPI ULBP2 was recognised by NKG2D and triggered NK cell cytotoxicity. These data show that differences in membrane attachment by NKG2D-ligands are more important for regulation of their surface expression than for cytotoxic recognition by NKG2D and emphasise that detailed characterization of the cell biology of individual NKG2Dligands will be necessary to allow targeted modulation of this system
DescriptionLola Fernández-Messina ...et al.
Publisher version (URL)http://dx.doi.org/10.1242/​jcs.076042
Appears in Collections:(CNB) Artículos
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