Work

O-GlcNAcase: Promiscuous Hexosaminidase or Key Regulator of O-GlcNAc Signaling?

Year: 2014

Type: review

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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.r114.609198

Authors: Jana Alonso, Marianne Schimpl, Daan M.F. van Aalten

Institutions: MRC Protein Phosphorylation and Ubiquitylation Unit, Medical Research Council, University of Dundee

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $1,916

Funder: Wellcome Trust