Chemical tools to explore nutrient-driven O-GlcNAc cycling. (July 2014)

• Record Type: Journal Article
• Authors: Kim, Eun J.; Bond, Michelle R.; Love, Dona C.; Hanover, John A.
• Is Part Of: Critical reviews in biochemistry and molecular biology. Volume 49:Number 4(2014:Jul./Aug.)
• Page Start: 327
• Page End: 342
• Publication Date: 2014-07
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Biochemistry -- Periodicals; Molecular Biology -- Periodicals; Review Literature -- Periodicals; 572
• DOI: 10.3109/10409238.2014.931338
• Languages: English
• ISSNs: 1040-9238

Abstract

<abstract> <title>Abstract</title> <p>Posttranslational modifications (PTM) including glycosylation, phosphorylation, acetylation, methylation and ubiquitination dynamically alter the proteome. The evolutionarily conserved enzymes <italic>O</italic>-linked <italic>N</italic>-acetylglucosamine (<italic>O</italic>-GlcNAc) transferase (OGT) and <italic>O</italic>-GlcNAcase are responsible for the addition and removal, respectively, of the nutrient-sensitive PTM of protein serine and threonine residues with <italic>O</italic>-GlcNAc. Indeed, the <italic>O</italic>-GlcNAc modification acts at every step in the "central dogma" of molecular biology and alters signaling pathways leading to amplified or blunted biological responses. The cellular roles of OGT and the dynamic PTM <italic>O</italic>-GlcNAc have been clarified with recently developed chemical tools including high-throughput assays, structural and mechanistic studies and potent enzyme inhibitors. These evolving chemical tools complement genetic and biochemical approaches for exposing the underlying biological information conferred by <italic>O</italic>-GlcNAc cycling.</p> </abstract>