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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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O-GlcNAcylation dictates pyroptosis.

Yue Lang1,2, Jincheng Li2, Leiliang Zhang1,2

  • 1Department of Clinical Laboratory Medicine, The First Affiliated Hospital of Shandong First Medical University and Shandong Provincial Qianfoshan Hospital, Jinan, Shandong, China.

Frontiers in Immunology
|January 1, 2025
PubMed
Summary
This summary is machine-generated.

O-GlcNAcylation regulates pyroptosis signaling. Enhancing O-GlcNAcylation of Gasdermin D (GSDMD) may improve sepsis outcomes and target inflammatory diseases.

Keywords:
GSDMDGSDMENLRP3O-GlcNAcylationpyroptosis

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Area of Science:

  • Biochemistry
  • Cellular Biology
  • Immunology

Background:

  • O-GlcNAcylation is a critical post-translational modification.
  • Pyroptosis is a key inflammatory cell death pathway.
  • Dysregulated pyroptosis contributes to various diseases.

Purpose of the Study:

  • To review the role of O-GlcNAcylation in pyroptosis signaling pathways.
  • To explore the therapeutic potential of modulating O-GlcNAcylation in inflammatory conditions.

Main Methods:

  • Literature review of O-GlcNAcylation and pyroptosis.
  • Analysis of O-GlcNAcylation's impact on key pyroptosis regulators like GSDMD, GSDME, NLRP3, NEK7, and NF-κB.

Main Results:

  • O-GlcNAcylation of GSDMD modulates pyroptosis, potentially improving sepsis-induced hypoperfusion.
  • O-GlcNAcylation of GSDME by high glucose promotes macrophage pyroptosis in periodontitis.
  • O-GlcNAcylation affects the NLRP3 inflammasome and its associated proteins.

Conclusions:

  • O-GlcNAcylation plays a significant role in the pathogenesis of sepsis, periodontitis, and osteoarthritis.
  • Targeting O-GlcNAcylation offers a promising therapeutic strategy for inflammatory diseases.