Protein ubiquitination is modulated by O‐GlcNAc glycosylation

@article{Guinez2008ProteinUI,
  title={Protein ubiquitination is modulated by O‐GlcNAc glycosylation},
  author={C{\'e}line Guinez and A M Mir and Vanessa Dehennaut and René Cacan and Anne Harduin-Lepers and Jean Claude Michalski and Tony Lefebvre},
  journal={The FASEB Journal},
  year={2008},
  volume={22},
  pages={2901 - 2911}
}
During the past two decades, O‐GlcNAc modification of cytosolic and nuclear proteins has been intensively studied. Nevertheless, the function of this post‐translational modification remains unclear. It has been recently speculated that O‐GlcNAc could act as a protective signal against proteasomal degradation, both by modifying target substrates and/or by inhibiting the proteasome itself. In this work, we have investigated the putative relation between O‐GlcNAc and the ubiquitin pathway. First… Expand
O-GlcNAc regulates NEDD4-1 stability via caspase-mediated pathway.
TLDR
This study reveals a regulation mechanism of NEDD4-1 stability by O-GlcNAcylation, and indirectly targets a vital E3 ubiquitin ligase enzyme of N EDD 4-1. Expand
Three Decades of Research on O-GlcNAcylation – A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism
  • G. Hart
  • Biology, Medicine
  • Front. Endocrinol.
  • 2014
TLDR
Progress has been made toward elucidating the specific functions of O-GlcNAcylation in essential cellular processes as well as the etiology of major human diseases of aging, such as diabetes, cancer, and neurodegeneration. Expand
Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis
TLDR
The regulation of these processes by O-GlcNAc and the impact of such regulation on survival in models of ischemia reperfusion injury and trauma hemorrhage are discussed. Expand
Functional O-GlcNAc modifications: Implications in molecular regulation and pathophysiology
TLDR
The following review intends to focus primarily on studies in the last half decade linking O-GlcNAc modification of proteins with chromatin-directed gene regulation, developmental processes, and several metabolically related disorders including Alzheimer's, heart disease and cancer. Expand
O-linked β-N-acetylglucosamine modification and its biological functions
TLDR
The recent advances on O-GlcNAc modification and its biological functions in animals and plants are summarized, and prospect of more special functions of O- GloverNAc will be revealed in plants is revealed. Expand
Regulation of Protein Degradation by O-GlcNAcylation: Crosstalk with Ubiquitination*
TLDR
This review summary of the current knowledge of the interplay between O-GlcNAcylation and ubiquitination in the control of protein degradation shall facilitate the development of therapeutics for human diseases such as cancer, metabolic syndrome, and neurodegenerative diseases. Expand
O-GlcNAcylation/Phosphorylation Cycling at Ser10 Controls Both Transcriptional Activity and Stability of Δ-Lactoferrin*
TLDR
It is shown that Ser10 is O-GlcNAcylated and that this modification is associated with increased ΔLf stability, achieved by blocking ubiquitin-dependent proteolysis, demonstrating that O- GloverNAcylation protects against polyubiquitination. Expand
Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O‐GlcNAc)
TLDR
This Review will highlight critical discoveries that shaped the understanding of the molecular events underpinning the impact of O‐GlcNAc on protein function, the role that O‐FlgNAc plays in maintaining cellular homeostasis, and the mechanisms that regulate O‐ Glc NAc‐cycling. Expand
O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains.
TLDR
These findings set the stage to assess whether O-GlcNAcylation has a role in protein quality control in a manner that bears similarity with the role played by N-glycosylation within the secretory pathway. Expand
O-Linked N-Acetylglucosamine Transiently Elevates in HeLa Cells during Mitosis
TLDR
It is observed that O-GlcNAc levels are significantly increased during mitosis in comparison to the other cell cycle phases, but this change could only be detected when mitotic cells were enriched by harvesting round shaped cells from the G2/M fraction of the synchronized cells. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 30 REFERENCES
Cytosolic O‐glycosylation is abundant in nerve terminals
TLDR
The activity and expression of O‐GlcNAc transferase and N‐acetyl‐β‐d‐glucosaminidase, the two enzymes regulating O‐ Glc NAc modifications, are present in nerve terminal structures (synaptosomes) and are particularily abundant in the cytosol of synaptosome proteins. Expand
Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.
TLDR
It is found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein. Expand
The Hexosamine Signaling Pathway: Deciphering the "O-GlcNAc Code"
TLDR
This review will begin to answer how the enzymes of O-GlcNAc cycling are regulated and how the cycle may interface with other cellular signaling pathways. Expand
Modulation of HSP70 GlcNAc-directed lectin activity by glucose availability and utilization.
TLDR
It is demonstrated that low glucose concentration, inhibition of glucose utilization with 2DG, or inhibition of sugars transport with CytB led to an increase of Hsp70 and Hsc70 lectin activities and also demonstrates that HSP70 does not regulate its GlcNAc-binding properties through its own O-Glc NAc glycosylation. Expand
70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine.
TLDR
The results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members. Expand
O-GlcNAc Modification Is an Endogenous Inhibitor of the Proteasome
TLDR
This work describes another means of controlling proteasome function in a global manner with reversible modification with the enzyme, O-GlcNAc transferase (OGT), which inhibits the proteolysis of the transcription factor Sp1 and a hydrophobic peptide through inhibition of the ATPase activity of 26S proteasomes. Expand
O-GlcNAc modification: a nutritional sensor that modulates proteasome function.
TLDR
This work has shown 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, suggesting a new model of proteasomal regulation. Expand
Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification.
TLDR
Recent studies demonstrate a role for O-GlcNAcylation in processes as diverse as transcription in the nucleus and signaling in the cytoplasm, suggesting that O- GlcNAc has both protein and site-specific influences on biochemistry and metabolism throughout the cell. Expand
O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress.
TLDR
The rapid and dynamic change in O-GlcNAc levels in response to extracellular stimuli, morphogens, the cell cycle and development suggests a key role for O- GloverNAc in signal transduction pathways. Expand
Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
TLDR
The results indicate that the dynamic interplay between O-GlcNAc and O-phosphate modifications coordinately regulate p53 stability and activity and stabilizes p53 by blocking ubiquitin-dependent proteolysis. Expand
...
1
2
3
...