Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins

Gerald Warren Hart, Michael P. Housley, Chad Slawson

Research output: Contribution to journalArticle

Abstract

All animals and plants dynamically attach and remove O-linked β-N-acetylglucosamine (O-GlcNAc) at serine and threonine residues on myriad nuclear and cytoplasmic proteins. O-GlcNAc cycling, which is tightly regulated by the concerted actions of two highly conserved enzymes, serves as a nutrient and stress sensor. On some proteins, O-GlcNAc competes directly with phosphate for serine/threonine residues. Glycosylation with O-GlcNAc modulates signalling, and influences protein expression, degradation and trafficking. Emerging data indicate that O-GlcNAc glycosylation has a role in the aetiology of diabetes and neurodegeneration.

Original languageEnglish (US)
Pages (from-to)1017-1022
Number of pages6
JournalNature
Volume446
Issue number7139
DOIs
StatePublished - Apr 26 2007

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins'. Together they form a unique fingerprint.

  • Cite this

    Hart, G. W., Housley, M. P., & Slawson, C. (2007). Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature, 446(7139), 1017-1022. https://doi.org/10.1038/nature05815