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

Jana Alonso; Marianne Schimpl; Daan M. F. van Aalten

doi:10.1074/jbc.R114.609198

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

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

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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 language	English
Pages (from-to)	34433-34439
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	289
Issue number	50
Early online date	21 Oct 2014
DOIs	https://doi.org/10.1074/jbc.R114.609198
Publication status	Published - 12 Dec 2014

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10.1074/jbc.R114.609198

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Aref#d: 21559. Molecular Mechanisms of Fungal Cell Wall Assembly (Programme Grant)
van Aalten, D. (Investigator)
Medical Research Council
1/11/09 → 31/10/14
Project: Research
Aref#d: 21318. Molecular Mechanisms of O-GlcNAc Signalling (Senior Fellowship Renewal)
van Aalten, D. (Investigator)
1/06/09 → 29/02/16
Project: Research

Cite this

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title = "O-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signalling?",

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.",

author = "Jana Alonso and Marianne Schimpl and {van Aalten}, {Daan M. F.}",

note = "Copyright {\textcopyright} 2014, The American Society for Biochemistry and Molecular Biology.",

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AU - Schimpl, Marianne

AU - van Aalten, Daan M. F.

PY - 2014/12/12

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AB - 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.

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

Abstract

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Projects

Aref#d: 21559. Molecular Mechanisms of Fungal Cell Wall Assembly (Programme Grant)

Aref#d: 21318. Molecular Mechanisms of O-GlcNAc Signalling (Senior Fellowship Renewal)

Cite this