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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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...
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Protein Glycosylation01:25

Protein Glycosylation

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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.
Glycosylation occurs in...
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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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Proteoglycans01:05

Proteoglycans

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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,...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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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.
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...
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Other Glycolytic Pathways01:24

Other Glycolytic Pathways

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The pentose phosphate pathway (PPP) operates in parallel with glycolysis, facilitating the metabolism of both pentoses and glucose. This pathway consists of two distinct phases: the oxidative and non-oxidative phases. While it does not directly generate ATP, the intermediates formed during the process can integrate into glycolysis, contributing to cellular energy metabolism when required.Oxidative Phase: NADPH ProductionThe oxidative phase of the pentose phosphate pathway is primarily...
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Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
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Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells

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SnapShot: N-Glycosylation Processing Pathways across Kingdoms.

Cheng-Yu Chung1, Natalia I Majewska1, Qiong Wang1

  • 1Department of Chemical and Biomolecular Engineering, The Johns Hopkins University, Baltimore, MD 21218, USA.

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|September 23, 2017
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Summary
This summary is machine-generated.

This study explores protein glycosylation, a key process where carbohydrates are added to proteins. Understanding these pathways is crucial for deciphering protein function and localization across diverse organisms.

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

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Post-translational modification (PTM) of proteins significantly impacts their biological roles.
  • Protein glycosylation, the addition of carbohydrate moieties, is a critical PTM affecting protein localization and function.
  • The variability and complexity of glycans present challenges in understanding their precise roles.

Purpose of the Study:

  • To present a concise overview of the core pathways involved in protein glycosylation.
  • To highlight conserved and divergent mechanisms of glycan installation across different organisms.
  • To provide a foundational resource for researchers studying protein glycosylation.

Main Methods:

  • Review and synthesis of existing literature on protein glycosylation pathways.
  • Comparative analysis of glycosylation mechanisms across various model organisms.
  • Focus on the enzymatic machinery responsible for glycan synthesis and transfer.

Main Results:

  • Identification of conserved core pathways for glycan precursor synthesis.
  • Description of diverse enzymatic strategies for glycan chain elongation and branching.
  • Highlighting organism-specific variations in glycan structures and their assembly.

Conclusions:

  • Protein glycosylation pathways are fundamental to cellular processes.
  • Understanding these pathways is essential for interpreting protein function and localization.
  • This overview serves as a guide to the complexity of glycan biosynthesis across life.