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This editorial refers to ‘ O -GlcNAcylation contributes to the vascular effects of ET-1 via activation of the RhoA/Rho-kinase pathway’ by V.V. Lima et al. , pp. 614–622, this issue. Post-translational modification of proteins is a common mechanism for the modulation of protein function, location, and turnover, and protein phosphorylation is probably the most widely studied form of post-translational modification. However, there is an increasing interest in modification of serine/threonine residues by the O -linked attachment of the monosaccharide β- N -acetyl-glucosamine ( O -GlcNAc); this is referred to as protein O -GlcNAcylation, to contrast it with traditional N- and O -glycosylation within the secretory pathways. Similar to phosphorylation, O -GlcNAc modification of proteins alters their function, activity, subcellular localization, and stability. Furthermore, since the same residues can be targets for both phosphorylation and O -GlcNAcylation, there is clearly a potential for direct interactions between them ( Figure 1 A ).1 Figure 1 ( A ) O -linked attachment of the GlcNAc (G) moiety to nuclear and cytosolic proteins is catalysed by O -GlcNAc transferase (OGT) and the removal catalysed by O -GlcNAcase (OGA), a process that is similar to and can interact with phosphorylation (P). ( B ) Summary of the positive and negative effects of O -GlcNAc signalling in the cardiovascular system as described in more detail in the following reviews.7–9The study by Lima et al .2 focuses on the intersection of endothelin (ET-1) signalling and regulation of protein O -GlcNAcylation and their effects on vascular reactivity. They showed that both ET-1 treatment …

The paradoxical world of protein O-GlcNAcylation: a novel effector of cardiovascular (dys)function