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Related Concept Videos

Structure of Cadherins01:25

Structure of Cadherins

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 diversity of cadherins...
Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

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.
Cell Sorting During Development
Cell sorting plays an...
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,...
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...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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Published on: October 17, 2014

Modulation of E-cadherin function and dysfunction by N-glycosylation.

Salomé S Pinho1, Raquel Seruca, Fátima Gärtner

  • 1Institute of Molecular Pathology and Immunology University of Porto, Portugal.

Cellular and Molecular Life Sciences : CMLS
|November 25, 2010
PubMed
Summary

E-cadherin dysfunction in cancer may stem from post-translational modifications, specifically N-glycosylation. This review explores how altering N-linked glycans on E-cadherin impacts its adhesive function, offering insights into cancer progression.

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Area of Science:

  • Molecular Biology
  • Cancer Research
  • Glycobiology

Background:

  • E-cadherin is crucial for cell adhesion and its dysfunction is implicated in cancer.
  • Genetic and epigenetic alterations explain some E-cadherin dysfunction, but many cases remain unexplained.
  • Post-translational modifications are increasingly recognized as critical regulators of protein function.

Purpose of the Study:

  • To review the molecular mechanisms of E-cadherin N-glycosylation.
  • To present evidence linking N-glycan modification of E-cadherin to its adhesive function.
  • To discuss the role of specific glycosyltransferases in E-cadherin N-glycosylation.

Main Methods:

  • Literature review focusing on E-cadherin glycosylation.
  • Analysis of studies investigating the impact of N-glycan structures on E-cadherin function.
  • Discussion of key enzymes involved in N-glycan remodeling.

Main Results:

  • N-glycosylation of E-cadherin is a significant post-translational modification.
  • Alterations in E-cadherin N-glycans can modulate its adhesive properties.
  • Specific glycosyltransferases, such as GnT-III, GnT-V, and FUT8, play roles in this process.

Conclusions:

  • N-glycosylation represents a critical post-translational regulatory mechanism for E-cadherin.
  • Dysfunctional E-cadherin in carcinomas may be partly explained by aberrant N-glycosylation.
  • Targeting glycosylation pathways could offer novel therapeutic strategies for cancer.