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O-GlcNAc signalling is regulated by an opposing pair of enzymes: O-GlcNAc transferase (OGT) instals, and O-GlcNAcase (OGA) removes the modification from proteins. The dynamics and the 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 review charts the discovery and the functional and structural analysis of OGA, and summarises 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.