Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D

Louise Bacon, Robert A Eagle, Martina Meyer, Nicholas Easom, Neil Thomas Young, John Trowsdale

Research output: Contribution to journalArticlepeer-review

147 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)1078-1084
Number of pages7
JournalThe Journal of Immunology
Issue number2
Publication statusPublished - 15 Jul 2004


  • Alternative Splicing
  • Amino Acid Sequence
  • Carrier Proteins
  • Cytomegalovirus
  • Histocompatibility Antigens Class I
  • Humans
  • Killer Cells, Natural
  • Ligands
  • Membrane Proteins
  • Molecular Sequence Data
  • Multigene Family
  • NK Cell Lectin-Like Receptor Subfamily K
  • Phylogeny
  • Protein Isoforms
  • Receptors, Immunologic
  • Receptors, Natural Killer Cell
  • Viral Proteins


Dive into the research topics of 'Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D'. Together they form a unique fingerprint.

Cite this