Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D
The Journal of Immunology, 2004•journals.aai.org
We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and
RAET1G. The encoded proteins were similar to the ULBP in their class I-like α1 and α2
domains, but differed in that, instead of being GPI-anchored, their sequences were type 1
membrane-spanning molecules. Both proteins were capable of being expressed at the cell
surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the
human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different …
RAET1G. The encoded proteins were similar to the ULBP in their class I-like α1 and α2
domains, but differed in that, instead of being GPI-anchored, their sequences were type 1
membrane-spanning molecules. Both proteins were capable of being expressed at the cell
surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the
human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different …
Abstract
We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and RAET1G. The encoded proteins were similar to the ULBP in their class I-like α1 and α2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both proteins were capable of being expressed at the cell surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different tissues and with different properties is consistent with multiple modes of infection-or stress-induced activation.
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