O-GlcNAc modification: A nutritional sensor that modulates proteasome function

Natasha E Zachara, Gerald Warren Hart

Research output: Contribution to journalArticle

Abstract

The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification of nucleocytoplasmic proteins that is thought to act in a manner analogous to protein phosphorylation. Recent work shows that many proteins of the metazoan proteasome are modified by O-GlcNAc and that the level of glycosylation is responsive to the nutritional state of the cell. Moreover, increased glycosylation of the 19S (or PA700) regulatory subcomplex has been correlated with decreased proteasomal activity, suggesting a new model of proteasomal regulation.

Original languageEnglish (US)
Pages (from-to)218-221
Number of pages4
JournalTrends in Cell Biology
Volume14
Issue number5
DOIs
StatePublished - May 2004

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Proteasome Endopeptidase Complex
Glycosylation
Acetylglucosamine
Threonine
Post Translational Protein Processing
Serine
Proteins
Phosphorylation

ASJC Scopus subject areas

  • Cell Biology

Cite this

O-GlcNAc modification : A nutritional sensor that modulates proteasome function. / Zachara, Natasha E; Hart, Gerald Warren.

In: Trends in Cell Biology, Vol. 14, No. 5, 05.2004, p. 218-221.

Research output: Contribution to journalArticle

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