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

by: L Bacon, RA Eagle, M Meyer, N Easom, NT Young, J Trowsdale

J Immunol, Vol. 173, No. 2. (15 July 2004), pp. 1078-1084.

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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 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.

@article{citeulike:1475240, 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 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.}, address = {Department of Pathology, Cambridge Institute for Medical Research, Addenbrookes Hospital, Cambridge, United Kingdom. lb117@cam.ac.uk}, author = {Bacon, L. and Eagle, R. A. and Meyer, M. and Easom, N. and Young, N. T. and Trowsdale, J. }, citeulike-article-id = {1475240}, issn = {0022-1767}, journal = {J Immunol}, keywords = {human, ligands, raet1, rafts, transmembrane, ulbp}, month = {July}, number = {2}, pages = {1078--1084}, posted-at = {2007-07-23 15:55:39}, priority = {2}, title = {Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/15240696}, volume = {173}, year = {2004} }

RIS record

TY - JOUR ID - citeulike:1475240 L3 - citeulike-article-id:1475240 TI - Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D. JF - J Immunol VL - 173 IS - 2 SP - 1078 EP - 1084 AD - Department of Pathology, Cambridge Institute for Medical Research, Addenbrookes Hospital, Cambridge, United Kingdom. lb117@cam.ac.uk SN - 0022-1767 N2 - 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. KW - human KW - ligands KW - raet1 KW - rafts KW - transmembrane KW - ulbp AU - Bacon, L AU - Eagle, RA AU - Meyer, M AU - Easom, N AU - Young, NT AU - Trowsdale, J PY - 2004/07/15/ UR - http://view.ncbi.nlm.nih.gov/pubmed/15240696 ER -

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