| First Author | Moody AM | Year | 2001 |
| Journal | Cell | Volume | 107 |
| Issue | 4 | Pages | 501-12 |
| PubMed ID | 11719190 | Mgi Jnum | J:72923 |
| Mgi Id | MGI:2154002 | Doi | 10.1016/s0092-8674(01)00577-3 |
| Citation | Moody AM, et al. (2001) Developmentally Regulated Glycosylation of the CD8alphabeta Coreceptor Stalk Modulates Ligand Binding. Cell 107(4):501-12 |
| abstractText | The functional consequences of glycan structural changes associated with cellular differentiation are ill defined. Herein, we investigate the role of glycan adducts to the O-glycosylated polypeptide stalk tethering the CD8alphabeta coreceptor to the thymocyte surface. We show that immature CD4(+)CD8(+) double-positive thymocytes bind MHCI tetramers more avidly than mature CD8 single-positive thymocytes, and that this differential binding is governed by developmentally programmed O-glycan modification controlled by the ST3Gal-I sialyltransferase. ST3Gal-I induction and attendant core 1 sialic acid addition to CD8beta on mature thymocytes decreases CD8alphabeta-MHCI avidity by altering CD8alphabeta domain-domain association and/or orientation. Hence, glycans on the CD8beta stalk appear to modulate the ability of the distal binding surface of the dimeric CD8 globular head domains to clamp MHCI. |
