Metabolic flux control in glycosylation.
Glycosylation is a common post-translational protein modification, in which glycans are built onto proteins through the sequential addition of monosaccharide units, in reactions catalysed by glycosyltransferases. Glycosylation influences the physicochemical and biological properties of proteins, with subsequent effects on subcellular and extracellular protein trafficking, cell-cell recognition, and ligand-receptor interactions. Glycan structures can be complex, as is the regulation of their biosynthesis, and it is only recently that the systems biology of metabolic flux control and glycosyltransferase networks has become a study in its own right. We review various models of glycosylation that have been proposed to date, based on current knowledge of Golgi structure and function, and consider how metabolic flux through glycosyltransferase networks regulates glycosylation events in the cell.
School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Andrew G
AG
McDonald
School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Jerrard M
JM
Hayes
School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland. Electronic address: gdavey@tcd.ie.
Gavin P
GP
Davey
D000818:Animals; D004798:Enzymes / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D064688:Metabolic Flux Analysis / Q000379:methods*; D008954:Models, Biological
D004798:Enzymes