| First Author | Goodall KJ | Year | 2021 |
| Journal | J Biol Chem | Volume | 297 |
| Issue | 4 | Pages | 101141 |
| PubMed ID | 34478713 | Mgi Jnum | J:313037 |
| Mgi Id | MGI:6793850 | Doi | 10.1016/j.jbc.2021.101141 |
| Citation | Goodall KJ, et al. (2021) Ribosylation of the CD8alphabeta heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10. J Biol Chem 297(4):101141 |
| abstractText | The CD8alphabeta heterodimer plays a crucial role in the stabilization between major histocompatibility complex class I molecules (MHC-I) and the T cell receptor (TCR). The interaction between CD8 and MHC-I can be regulated by posttranslational modifications, which are proposed to play an important role in the development of CD8 T cells. One modification that has been proposed to control CD8 coreceptor function is ribosylation. Utilizing NAD(+), the ecto-enzyme adenosine diphosphate (ADP) ribosyl transferase 2.2 (ART2.2) catalyzes the addition of ADP-ribosyl groups onto arginine residues of CD8alpha or beta chains and alters the interaction between the MHC and TCR complexes. To date, only interactions between modified CD8 and classical MHC-I (MHC-Ia), have been investigated and the interaction with non-classical MHC (MHC-Ib) has not been explored. Here, we show that ADP-ribosylation of CD8 facilitates the binding of the liver-restricted nonclassical MHC, H2-Q10, independent of the associated TCR or presented peptide, and propose that this highly regulated binding imposes an additional inhibitory leash on the activation of CD8-expressing cells in the presence of NAD(+). These findings highlight additional important roles for nonclassical MHC-I in the regulation of immune responses. |
