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Updated: Apr 21, 2026

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
Published on: April 27, 2010
O-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signaling?
Jana Alonso1, Marianne Schimpl1, Daan M F van Aalten2
1From the Medical Research Council Protein Phosphorylation and Ubiquitylation Unit and.
Abstract:
O-GlcNAc signaling is regulated by an opposing pair of enzymes: O-GlcNAc transferase installs and O-GlcNAcase (OGA) removes the modification from proteins. The dynamics and regulation of this process are only beginning to be understood as the physiological functions of both enzymes are being probed using genetic and pharmacological approaches. This minireview charts the discovery and functional and structural analysis of OGA and summarizes the insights gained from recent studies using OGA inhibition, gene knock-out, and overexpression. We identify several areas of "known unknowns" that would benefit from future research, such as the enigmatic C-terminal domain of OGA.
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