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Oligosaccharide Assembly01:24

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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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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
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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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O-Mannose Glycosylations Influence E-Cadherin Functional Interactions.

Shaoshuai Xie1, Katarina Madunić2, Omar G Rosas Bringas3

  • 1European Research Institute for the Biology of Ageing, University Medical Center Groningen, Groningen, The Netherlands; National Glycoengineering Research Center, Shandong University, Qingdao, China.

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O-linked mannose (O-Man) modifications on E-cadherin (CDH1) impact its protein interactions. Ablating O-Man on specific cadherin domains alters CDH1

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E-cadherinO-mannose glycosylationTMTC enzymesaffinity proteomicsglycoproteomics

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Area of Science:

  • Molecular and Cellular Biology
  • Glycoscience
  • Proteomics

Background:

  • Cadherins are crucial for cell adhesion and signaling, with functions mediated by extracellular cadherin (EC) domains.
  • EC domains undergo N-linked and O-linked glycosylations, including O-linked mannose (O-Man) on conserved residues.
  • O-Man glycosylations are catalyzed by TMTC1-4 enzymes, with distinct enzymes targeting B- or G-strands.

Purpose of the Study:

  • To investigate the hypothesis that O-Man post-translational modifications (PTMs) fine-tune cadherin-mediated cellular adhesion and interactions.
  • To identify O-Man-dependent protein-protein interactions involving epithelial cadherin (E-cadherin, CDH1).

Main Methods:

  • Genetic ablation of O-Man glycans in model cells.
  • Affinity proteomics to assay for changes in protein-protein interactions with E-cadherin.
  • Orthogonal validation of altered associations, including between CDH1 and CDH3 (P-cadherin).

Main Results:

  • O-Man-dependent protein interactions of E-cadherin (CDH1) were identified.
  • Ablation of O-Man resulted in altered associations between CDH1 and other proteins, including CDH3.
  • Distinct interactomic changes were observed upon O-Man ablation on B- versus G-strands, indicating site-specific regulation.

Conclusions:

  • O-Man glycosylations play a significant role in regulating E-cadherin (CDH1) protein interactions.
  • The location of O-Man modification (B- vs. G-strands) influences the specific protein complexes formed by CDH1.
  • These findings provide novel insights into the regulatory mechanisms of cadherin function through O-Man glycosylation.