Mammalian O-mannosylation: unsolved questions of structure/function |
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Authors: | Stalnaker Stephanie H Stuart Ryan Wells Lance |
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Institution: | 1University of Georgia, Complex Carbohydrate Research Center, Athens, GA, United States;2University of Georgia, Department of Biochemistry and Molecular Biology, Athens, GA, United States |
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Abstract: | Post-translational modification of polypeptides with glycans increases the diversity of the structures of proteins and imparts increased functional diversity. Here, we review the current literature on a relatively new O-glycosylation pathway, the mammalian O-mannosylation pathway. The importance of O-mannosylation is illustrated by the fact that O-mannose glycan structures play roles in a variety of processes including viral entry into cells, metastasis, cell adhesion, and neuronal development. Furthermore, mutations in the enzymes of this pathway are causal for a variety of congenital muscular dystrophies. Here we highlight the protein substrates, glycan structures, and enzymes involved in O-mannosylation as well as our gaps in understanding structure/function relationships in this biosynthetic pathway. |
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