| First Author | Rybakin V | Year | 2011 |
| Journal | EMBO Rep | Volume | 12 |
| Issue | 12 | Pages | 1251-6 |
| PubMed ID | 22081144 | Mgi Jnum | J:314080 |
| Mgi Id | MGI:6810793 | Doi | 10.1038/embor.2011.209 |
| Citation | Rybakin V, et al. (2011) CD8alphaalpha and -alphabeta isotypes are equally recruited to the immunological synapse through their ability to bind to MHC class I. EMBO Rep 12(12):1251-6 |
| abstractText | Bimolecular fluorescence complementation was used to engineer CD8 molecules so that CD8alphaalpha and CD8alphabeta dimers can be independently visualized on the surface of a T cell during antigen recognition. Using this approach, we show that CD8alphaalpha is recruited to the immunological synapse almost as well as CD8alphabeta, but because the kinase Lck associates preferentially with CD8alphabeta in lipid rafts, CD8alphaalpha is the weaker co-receptor. During recognition of the strong CD8alphaalpha ligand H2-TL, CD8alphaalpha is preferentially recruited. Thus, recruitment of the two CD8 species correlates with their relative binding to the available ligands, rather than with the co-receptor functions of the CD8 species. |
