2024-03-28T12:45:15Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/472102021-07-28T09:58:55Zcom_10261_25com_10261_1col_10261_278
00925njm 22002777a 4500
dc
Reyburn, H. T.
author
Valés-Gómez, Mar
author
2011-02
The 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
Journal of Cell Science 124: 321-32 (2011)
0021-9533
http://hdl.handle.net/10261/47210
10.1242/jcs.07604
1477-9137
GPI-anchored proteins
NKG2D
Innate Immunity
DRMs
ER trafficking
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