Two Human ULBP/RAET1 Molecules with Transmembrane Regions Are Ligands for NKG2D

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 alpha1 and alpha2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both prot...

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Bibliographic Details
Published in:The Journal of immunology (1950) 2004-07, Vol.173 (2), p.1078-1084
Main Authors: Bacon, Louise, Eagle, Robert A, Meyer, Martina, Easom, Nicholas, Young, Neil T, Trowsdale, John
Format: Article
Language:English
Subjects:
Alternative Splicing
Amino Acid Sequence
Carrier Proteins - metabolism
Cytomegalovirus - metabolism
Histocompatibility Antigens Class I - metabolism
Humans
Killer Cells, Natural - metabolism
Ligands
Membrane Proteins - metabolism
Molecular Sequence Data
Multigene Family
NK Cell Lectin-Like Receptor Subfamily K
Phylogeny
Protein Isoforms
Receptors, Immunologic - metabolism
Receptors, Natural Killer Cell
Viral Proteins - metabolism
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Summary: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 alpha1 and alpha2 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.
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.173.2.1078