Journal
CELL
Volume 107, Issue 4, Pages 501-512Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(01)00577-3
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Funding
- NHLBI NIH HHS [HL57345] Funding Source: Medline
- NIAID NIH HHS [AI19807, AI45022] Funding Source: Medline
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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 CD8 alpha beta 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-1 sialyltransferase. ST3Gal-1 induction and attendant core 1 sialic acid addition to CD8 beta on mature thymocytes decreases CD8 alpha beta -MHCI avidity by altering CD8 alpha beta domain-domain association and/or orientation. Hence, glycans on the CD8 beta stalk appear to modulate the ability of the distal binding surface of the dimeric, CD8 globular head domains to clamp MHCI.
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