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- Title
Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation
- Authors
Hu, Ping; Shimoji, Shino; Hart, Gerald W.
- Abstract
Abstract: Ser(Thr)-O-linked β-N-acetylglucosamine (O-GlcNAc) is a ubiquitous modification of nucleocytoplasmic proteins. Extensive crosstalk exists between O-GlcNAcylation and phosphorylation, which regulates signaling in response to nutrients/stress. The development of novel O-GlcNAc detection and enrichment methods has improved our understanding of O-GlcNAc functions. Mass spectrometry has revealed O-GlcNAc’s many interactions with phosphorylation-mediated signaling. However, mechanisms regulating O-GlcNAcylation and phosphorylation are quite different. Phosphorylation is catalyzed by hundreds of distinct kinases. In contrast, in mammals, uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyl transferase (OGT) and β-D-N-acetylglucosaminidase (OGA) are encoded by single highly conserved genes. Both OGT’s and OGA’s specificities are determined by their transient associations with many other proteins to create a multitude of specific holoenzymes. The extensive crosstalk between O-GlcNAcylation and phosphorylation represents a new paradigm for cellular signaling.
- Subjects
CELLULAR control mechanisms; PHOSPHORYLATION; GLUCOSAMINE; ACYLATION; CELLULAR signal transduction; MASS spectrometry; ADENOSINE triphosphate; ESTROGEN receptors
- Publication
FEBS Letters, 2010, Vol 584, Issue 12, p2526
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2010.04.044