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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...
Canonical Wnt Signaling Pathway02:54

Canonical Wnt Signaling Pathway

The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which results in tumor...
Canonical Wnt Signaling Pathway02:54

Canonical Wnt Signaling Pathway

The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which results in tumor...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Notch Signaling Pathway03:14

Notch Signaling Pathway

The Notch signaling pathway is a major intracellular signaling pathway that is highly conserved over a broad spectrum of metazoan species. It stands unique from other intracellular signaling mechanisms in animals because notch protein itself acts as the receptor as well as the primary signaling molecule.
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not until 1985...

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Differentiation of Mouse Breast Epithelial HC11 and EpH4 Cells
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Classical cadherins control survival through the gp130/Stat3 axis.

M Geletu1, R Arulanandam, S Chevalier

  • 1Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada.

Biochimica Et Biophysica Acta
|April 2, 2013
PubMed
Summary

Cadherin engagement, including E-cadherin, N-cadherin, and cadherin-11, activates Signal Transducer and Activator of Transcription-3 (Stat3), promoting cell survival and proliferation. This contrasts with Erk pathway activity, which is inhibited by cadherin engagement.

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Differentiation of Mouse Breast Epithelial HC11 and EpH4 Cells
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Signal Transducer and Activator of Transcription-3 (Stat3) is a key signaling molecule activated by various kinases.
  • E-cadherin engagement was previously shown to activate Stat3.
  • Classical cadherins play roles in cell adhesion and are implicated in cancer metastasis.

Purpose of the Study:

  • To investigate the effect of cadherin-11 and N-cadherin engagement on Stat3 phosphorylation and activity.
  • To explore the role of IL6 family cytokines in cadherin-mediated Stat3 activation.
  • To examine the impact of cadherin engagement on Extracellular Signal Regulated kinase (Erk) activity.

Main Methods:

  • Assessing Stat3 and Erk phosphorylation and activity upon engagement of cadherin-11 and N-cadherin.
  • Analyzing the role of IL6 family cytokines in Stat3 activation.
  • Utilizing cadherin-11 knock-down experiments to study Erk activation.

Main Results:

  • Engagement of cadherin-11 and N-cadherin triggers a significant increase in Stat3 activity, mediated by IL6 family cytokines.
  • Cadherin-11 engagement activates Stat3, which is essential for cell survival, proliferation, and migration.
  • Unlike Stat3, Erk activity is unaffected by cadherin-11 engagement; cadherin engagement inhibits IL6-induced Erk activation in dense cultures.

Conclusions:

  • Classical cadherins (E-cadherin, N-cadherin, cadherin-11) consistently activate Stat3, suggesting Stat3 acts as a central survival factor.
  • Cadherin engagement plays a regulatory role in the Erk signaling pathway, distinct from its effect on Stat3.
  • Stat3 activation by cadherins may be a fundamental mechanism for cell survival across various tissues, irrespective of metastatic potential.