- Human pathology

Home > A. Molecular pathology > O-N-acetylglucosamine


Wednesday 27 May 2009

O-GlcNAc is added to serines or threonines by O-GlcNAc transferase. O-GlcNAc appears to occur on serines and threonines that would otherwise be phosphorylated by serine/threonine kinases. Thus, if phosphorylation occurs, O-GlcNAc does not, and vice versa.

This is an incredibly important finding because phosphorylation/dephosphorylation has become a scientific paradigm for the regulation of signaling within cells.

A massive amount of cancer research is focused on phosphorylation. Ignoring the involvement of this form of glycosylation, which clearly appears to act in concert with phosphorylation, means that a lot of current research is missing at least half of the picture.

O-GlcNAc addition and removal also appear to be key regulators of the pathways that are deregulated in diabetes mellitus. The gene encoding the O-GlcNAc removal enzyme has been linked to non-insulin dependent diabetes mellitus.

It is the terminal step in a nutrient-sensing hexosamine signaling pathway.

See also

- glycosylation