CD45 glycosylation controls T-cell life and death
- Author(s): Earl, LA
- Baum, LG
- et al.
Published Web Locationhttp://www.nature.com/icb/journal/v86/n7/full/icb200846a.html
CD45, an abundant and highly glycosylated cell-surface protein, is a critical regulator of T-cell development. CD45 is differentially glycosylated throughout the life of a T cell, and the glycosylation state of CD45 controls recognition by various binding partners, affects intracellular signaling by the cytoplasmic tyrosine phosphatase domain and modulates the response of the T cell to antigen. Although the importance of CD45 during T-cell development has been established, it is becoming increasingly clear that glycosylation of CD45 is a dynamic process that modifies T-cell survival, activation and immune function. In this review, we address changes that occur in CD45 glycosylation during T-cell development and differentiation, describe carbohydrate-binding proteins that recognize differentially glycosylated forms of CD45, and discuss how differential glycosylation alters the T-cell response to a variety of signals involved in selection, activation and apoptosis. © 2008 Australasian Society for Immunology Inc. All rights reserved.
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