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Glycosylation is the most common posttranslational modification of proteins and consists of the addition of sugar moiety to proteins. The resulting glycosylated proteins are often secreted to the extracellular compartment or integrated into different cell organelles. This modification was identified in plant as well as in mammalian cells.  A number of plant and mammal proteins are either N- or O-glycosylated. This review focuses on O-glycosylation which refers to linkage of a glycan to hydroxyl group of serine, threonine or proline residues. O-glycosylation can be altered by the action of chemical inhibitors. For instance, 3,4-dehydro-L-proline, ethyl 3,4-dehydroxy benzoate and a,a-dipyridyl inhibit the activity of prolyl4-hydroxylase, a key enzyme for plant O-glycosylation. In addition, a small molecule inhibitor designated 1-68A inhibits the polypeptide N-acetylgalactosaminyltransferases of mammalian cells. The aim of this review is to summarize the role and mechanism of action of these inhibitors of O-glycosylation and their impact on cell development in plants and mammals.

O-glycosylation in plant and mammal cells: the use of chemical inhibitors to understand the biosynthesis and function of O-glycosylated proteins