Sweet 'n' sour: the impact of differential glycosylation on T cell responses.
The fate and functional activity of T lymphocytes depend largely on the precise timing of gene expression and protein production. However, it is clear that post-translational modification of proteins affects their functional properties. Although modifications such as phosphorylation have been intensely studied by immunologists, less attention has been paid to the impact that changes in glycosylation have on protein function. However, there is considerable evidence that glycosylation plays a key role in immune regulation. We will focus here on examples in which differential glycosylation affects the development, survival or reactivity of T cells.
D000818:Animals; D015703:Antigens, CD; D037161:Galectins; D006031:Glycosylation; D006388:Hemagglutinins / Q000276:immunology; D006801:Humans; D051917:Leukosialin; D008562:Membrane Glycoproteins / Q000276:immunology; D011499:Protein Processing, Post-Translational; D011948:Receptors, Antigen, T-Cell / Q000276:immunology; D011971:Receptors, Immunologic / Q000276:immunology; D019087:Selectins / Q000276:immunology; D063267:Sialic Acid Binding Ig-like Lectin 1; D012795:Sialoglycoproteins / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology*
D015703:Antigens, CD; D037161:Galectins; D006388:Hemagglutinins; D051917:Leukosialin; D008562:Membrane Glycoproteins; D011948:Receptors, Antigen, T-Cell; D011971:Receptors, Immunologic; C571166:SIGLEC1 protein, human; C465014:SPN protein, human; D019087:Selectins; D063267:Sialic Acid Binding Ig-like Lectin 1; D012795:Sialoglycoproteins