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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

Insights

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.

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.

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