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Related Concept Videos

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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation 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.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...

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Updated: May 24, 2026

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

Multiple post-translational modifications regulate E-cadherin transport during apoptosis.

Fei Geng1, Weijia Zhu, Richard A Anderson

  • 1Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.

Journal of Cell Science
|March 1, 2012
PubMed
Summary
This summary is machine-generated.

E-cadherin modifications, O-GlcNAcylation and incomplete processing, block its cell surface transport and accelerate apoptosis. These findings reveal new mechanisms regulating E-cadherin in response to cellular stress.

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Induction and Analysis of Epithelial to Mesenchymal Transition

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Related Experiment Videos

Last Updated: May 24, 2026

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Induction and Analysis of Epithelial to Mesenchymal Transition
10:37

Induction and Analysis of Epithelial to Mesenchymal Transition

Published on: August 27, 2013

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • E-cadherin is crucial for cell adhesion and preventing anoikis (apoptosis upon detachment).
  • Acute loss of E-cadherin sensitizes cells to apoptosis via unknown post-translational mechanisms.

Purpose of the Study:

  • To investigate novel post-translational modifications of E-cadherin that regulate its cell surface transport and impact apoptosis.
  • To elucidate the role of O-linked β-N-acetylglucosamine (O-GlcNAc) modification and proprotein convertase processing in E-cadherin function.

Main Methods:

  • Treatment of breast cancer cells with drugs.
  • Detection of E-cadherin modifications using specific lectins and antibodies.
  • Analysis of E-cadherin binding to catenins and PIPKIγ.
  • Utilizing deletion mutants to assess the impact of O-GlcNAcylation on PIPKIγ binding and cell surface transport.

Main Results:

  • O-GlcNAcylation retains E-cadherin in the endoplasmic reticulum, while incomplete proprotein convertase processing arrests it in the secretory pathway.
  • These modifications do not affect binding to α-catenin, β-catenin, or γ-catenin.
  • O-GlcNAcylation blocks E-cadherin binding to PIPKIγ, inhibiting plasma membrane trafficking and accelerating apoptosis.
  • Deletion mutants resistant to O-GlcNAcylation bind PIPKIγ, traffic to the cell surface, and delay apoptosis.

Conclusions:

  • O-GlcNAcylation of E-cadherin accelerates apoptosis by inhibiting its transport to the cell surface.
  • Cell-stress-induced inactivation of proprotein convertases exacerbates apoptosis by impairing E-cadherin maturation.
  • These modifications represent novel mechanisms for rapid E-cadherin regulation in response to cellular intoxication.