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CD45 Glycosylation controls T‐cell life and death
Author(s) -
Earl L A,
Baum L G
Publication year - 2008
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1038/icb.2008.46
Subject(s) - glycosylation , microbiology and biotechnology , protein tyrosine phosphatase , t cell , biology , cell , intracellular , programmed cell death , signal transduction , immune system , apoptosis , biochemistry , immunology
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.