CD45 glycosylation controls T-cell life and death.
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.
Earl
L A
LA
Department of Pathology and Laboratory Medicine, UCLA School of Medicine, University of California, Los Angeles, CA 90095, USA.
Baum
L G
LG
D000818:Animals; D016923:Cell Death; D006031:Glycosylation; D006801:Humans; D037102:Lectins / Q000378:metabolism; D017493:Leukocyte Common Antigens / Q000378:metabolism*; D008213:Lymphocyte Activation / Q000502:physiology; D013601:T-Lymphocytes / Q000166:cytology / Q000378:metabolism / Q000502:physiology*
D037102:Lectins; D017493:Leukocyte Common Antigens