Genetic defects in N-glycosylation and cellular diversity in mammals.
Glycoproteins in mammalian cells are modified with complex-type aspargine-linked glycans of variable chain lengths and composition. Observations of mice carrying mutations in glycosyltransferase genes imply that N-glycan structures regulate T-cell receptor clustering and hence sensitivity to agonists. We argue that the heterogeneity inherent in N-glycosylation contributes to cellular diversity and, thereby, to adaptability in the immune system.
Dennis
J W
JW
Department of Molecular & Medical Genetics, University of Toronto, Ontario, Canada. dennis@mshri.on.ca
Warren
C E
CE
Granovsky
M
M
Demetriou
M
M
D000818:Animals; D005314:Embryonic and Fetal Development; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D037102:Lectins / Q000378:metabolism; D008661:Metabolism, Inborn Errors / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D011134:Polysaccharides / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism; D015398:Signal Transduction
D006023:Glycoproteins; D037102:Lectins; D011134:Polysaccharides; D011948:Receptors, Antigen, T-Cell