A number of biologically active substances are "intimately associated" in a way that allows hypotheses to be made about their relationship with one another, say researchers.
Writing in Cell Communication and Signaling, Suresh Mishra, Sudharsana Ande and Neil Salter explain that phosphorylation in some proteins has been associated with beta-N-acetylglucosamine (O-GlcNAc) modification.
This in turn is mediated by the beta-N-acetylglucosamine transferase enzyme, adding to the interlinking between biologically active substances at play in the process.
While understanding of the mechanisms at work in O-GlcNAc modification is poor, the scientists propose that phosphorylation may in fact be a requisite part of the procedure.
This hypothesis is drawn from mass spectrometry analysis of O-GlcNAc modification sites in proteins conducted in recent years.
According to the scientists, their proposal facilitates understanding of how modification interplays with proteins' serine and threonine phosphorylation.
Cell Communication and Signaling addresses both translational and basic aspects of cellular mechanisms and is the official periodical of the Signal Transduction Society.
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