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A more recent version of this article appeared on July 1, 2004
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Submitted on November 3, 2003
Revised on April 16, 2004
Accepted on April 27, 2004
1 Receptor Cell Biology Section, Laboratory of Allergic Diseases, National Institute of Allergic and Infectious Diseases, National Institutes of Health. Rockville, MD 20852 (Present Address: Department of Cell Biology, Georgetown University, Washington, DC, 20007)
2 Receptor Cell Biology Section, Laboratory of Allergic Diseases, National Institute of Allergic and Infectious Diseases, National Institutes of Health. Rockville, MD 20852
* Corresponding author. E-mail address: Fborrego{at}niaid.nih.gov.
CD94/NKG2A is an inhibitory receptor expressed by most human natural killer (NK) cells and a subset of T cells that recognizes human leukocyte antigen E (HLA-E) on potential target cells. To elucidate the cell surface dynamics of CD94/NKG2A receptors, we have expressed CD94/NKG2A-EGFP receptors in the rat basophilic leukemia (RBL) cell line. Photobleaching experiments revealed that CD94/NKG2A-EGFP receptors move freely within the plasma membrane and accumulate at the site of contact with ligand. The enriched CD94/NKG2A-EGFP is markedly less mobile than the nonligated receptor. We observed that not only are lipid rafts not required for receptor polarization, they are excluded from the site of receptor contact with the ligand. Furthermore, the lipid raft patches normally observed at the sites where Fc
R1 activation receptors are cross-linked were not observed when CD94/NKG2A was coengaged along with the activation receptor. These results suggest that immobilization of the CD94/NKG2A receptors at ligation sites not only promote sustenance of the inhibitory signal, but by excluding lipid rafts exclusion prevents formation of activation signaling complexes.
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