| First Author | Stepp SE | Year | 1999 |
| Journal | Eur J Immunol | Volume | 29 |
| Issue | 8 | Pages | 2392-9 |
| PubMed ID | 10458751 | Mgi Jnum | J:56786 |
| Mgi Id | MGI:1342417 | Doi | 10.1002/(SICI)1521-4141(199908)29:08<2392::AID-IMMU2392>3.0.CO;2-R |
| Citation | Stepp SE, et al. (1999) Gene structure of the murine NK cell receptor 2B4: presence of two alternatively spliced isoforms with distinct cytoplasmic domains. Eur J Immunol 29(8):2392-9 |
| abstractText | The NK cell receptor 2B4 is expressed on the surface of all murine NK cells and a subset of T cells. Ligation of 2B4 with monoclonal antibodies increases target cell lysis and IFN-gamma production. 2B4 is the high-affinity counter-receptor for CD48 in mice and humans. 2B4-L is a member of the CD2 subgroup of the immunoglobulin supergene family, which includes CD48, LFA-3, CD84, Ly9 and SLAM. Here we describe 2B4-S, a second 2B4 isoform, and the genomic structure of the 2B4 gene. 2B4-S is identical to the 5' end of 2B4-L, differing only at the 3' end, corresponding to a portion of the cytoplasmic domain and the 3' untranslated sequence. Both 2B4-L and 2B4-S are expressed on IL-2-activated NK cells. The genomic clone of 2B4 reveals that the two cDNA clones are products of alternative splicing. Since they differ only in a portion of the cytoplasmic domain, it is likely that they transduce different signals. |
