O-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signalling?

Jana Alonso , Marianne Schimpl, Daan M. F. van Aalten (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    28 Citations (Scopus)
    142 Downloads (Pure)

    Abstract

    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.
    Original languageEnglish
    Pages (from-to)34433-34439
    Number of pages7
    JournalJournal of Biological Chemistry
    Volume289
    Issue number50
    Early online date21 Oct 2014
    DOIs
    Publication statusPublished - 12 Dec 2014

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