Structural Characterization of the O-GlcNAc Cycling Enzymes: Insights into Substrate Recognition and Catalytic Mechanisms

Overview

Journal Curr Opin Struct Biol

Date 2019 Feb 2

PMID 30708324

Citations 39

Authors

Cassandra M Joiner

Hao Li

Jiaoyang Jiang

Suzanne Walker

Affiliations

Soon will be listed here.

Abstract

Dysregulation of nuclear and cytoplasmic O-linked β-N-acetylglucosamine (O-GlcNAc) cycling is implicated in a range of diseases including diabetes and cancer. This modification maintains cellular homeostasis by regulating several biological processes, such as cell signaling. This highly regulated cycle is governed by two sole essential enzymes, O-GlcNAc transferase and O-GlcNAcase that add O-GlcNAc and remove it from over a thousand substrates, respectively. Until recently, due to lack of structural information, the mechanism of substrate recognition has eluted researchers. Here, we review recent successes in structural characterization of these enzymes and how this information has illuminated key features essential for catalysis and substrate recognition. Additionally, we highlight recent studies which have used this information to expand our understanding of substrate specificity by each enzyme.

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