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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.
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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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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Updated: Apr 21, 2026

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
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Xylose phosphorylation functions as a molecular switch to regulate proteoglycan biosynthesis.

Jianzhong Wen1, Junyu Xiao1, Meghdad Rahdar1

  • 1Departments of Pharmacology and.

Proceedings of the National Academy of Sciences of the United States of America
|October 22, 2014
PubMed
Summary

Family with sequence similarity 20, member B (Fam20B) phosphorylates xylose, acting as a molecular switch. This Fam20B-dependent phosphorylation regulates glycosaminoglycan assembly and is crucial for proteoglycan biosynthesis.

Keywords:
Fam20BGalT-IIproteoglycansecretory kinasexylose phosphorylation

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Proteoglycans are essential for intercellular signaling in eukaryotic cells.
  • The precise regulation of proteoglycan biosynthesis remains incompletely understood.
  • Key enzymes and regulatory mechanisms governing glycosaminoglycan chain assembly are critical.

Purpose of the Study:

  • To elucidate the role of Family with sequence similarity 20, member B (Fam20B) in proteoglycan biosynthesis.
  • To investigate how Fam20B regulates the initiation of glycosaminoglycan chain assembly.
  • To identify the molecular switch controlling subsequent glycosaminoglycan elongation.

Main Methods:

  • Utilized FAM20B knockout cells to analyze proteoglycan structure.
  • Investigated the effect of Fam20B-dependent xylose phosphorylation on enzyme activity.
  • Examined the functional consequences of inactivating mutations in the Galactosyl transferase II (GalT-II) gene (B3GALT6).

Main Results:

  • Fam20B phosphorylates the initiating xylose residue in the proteoglycan linkage region, acting as a regulatory switch.
  • FAM20B knockout cells produce proteoglycans with truncated linkage regions, preventing further glycosaminoglycan elongation.
  • Fam20B-dependent xylose phosphorylation significantly enhances the activity of Galactosyl transferase II (GalT-II).

Conclusions:

  • Fam20B-dependent xylose phosphorylation is a critical regulatory mechanism for proteoglycan biosynthesis.
  • Impaired GalT-II function due to loss of Fam20B-dependent phosphorylation leads to proteoglycan maturation defects.
  • This study reveals a novel pathway controlling glycosaminoglycan assembly and proteoglycan maturation.