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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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.
Glycosylation occurs in...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Protein Modifications in the RER01:26

Protein Modifications in the RER

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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

O-GlcNAc modifications regulate lamin A tail processing.

Katherine Augspurger1,2,3, Elizabeth Martin1,2, Jason Maynard4

  • 1Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, United States.

Biorxiv : the Preprint Server for Biology
|March 31, 2025
PubMed
Summary
This summary is machine-generated.

O-GlcNAcylation, a glucose-sensitive modification, promotes lamin A processing by enhancing tail cleavage. This finding links glucose metabolism to nuclear lamina biogenesis and lamin A regulation.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Lamin A processing is crucial for nuclear lamina assembly, nuclear structure, and chromatin organization.
  • Pre-lamin A undergoes farnesylation and C-terminal cleavage to yield mature lamin A.
  • O-GlcNAc Transferase (OGT) is a glucose-sensitive enzyme involved in post-translational modifications.

Purpose of the Study:

  • To investigate the role of OGT and O-GlcNAcylation in regulating lamin A biogenesis and processing.
  • To explore the potential link between glucose metabolism and nuclear lamina formation.

Main Methods:

  • Examined the effects of varying OGT levels and OGT inhibition on endogenous lamin A.
  • Utilized a modified tail cleavage assay to assess O-GlcNAcylation's direct impact on lamin A processing.
  • Introduced mutations in OGT binding motifs and O-GlcNAc modification sites.

Main Results:

  • Altering OGT levels or activity did not affect endogenous lamin A abundance or distribution.
  • Mutations disrupting OGT binding or O-GlcNAc modification sites reduced tail cleavage efficiency.
  • O-GlcNAcylation was found to promote lamin A processing, specifically tail cleavage.

Conclusions:

  • O-GlcNAcylation plays a promoting role in lamin A processing.
  • These findings establish a connection between glucose metabolism and nuclear lamina biogenesis.
  • Identified O-GlcNAcylation as a regulatory mechanism for lamin A cleavage.