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Related Concept Videos

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...
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...
Role Of Notch Signalling In Intestinal Stem Cell Renewal01:12

Role Of Notch Signalling In Intestinal Stem Cell Renewal

Notch signaling was first discovered in Drosophila melanogaster, where it is involved in cell lineage differentiation. Notch signaling regulates the maintenance and differentiation of intestinal stem cells or ISCs by controlling the expression of atonal homolog 1 or Atoh1. Atoh1 directs cells to differentiate into secretory cells.
Direct cell-to-cell contact is needed for the activation of Notch signaling. The signal is initiated when a notch ligand binds to a receptor on an adjacent cell, also...
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...
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...
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...

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Related Experiment Video

Updated: Jun 2, 2026

Cell Aggregation Assays to Evaluate the Binding of the Drosophila Notch with Trans-Ligands and its Inhibition by Cis-Ligands
05:48

Cell Aggregation Assays to Evaluate the Binding of the Drosophila Notch with Trans-Ligands and its Inhibition by Cis-Ligands

Published on: January 2, 2018

Role of STRAP in regulating GSK3β function and Notch3 stabilization.

Nilesh D Kashikar1, Wanguang Zhang, Pierre P Massion

  • 1Vanderbilt University School of Medicine, Nashville, TN USA.

Cell Cycle (Georgetown, Tex.)
|April 20, 2011
PubMed
Summary

The scaffold protein STRAP binds Glycogen synthase kinase 3β (GSK3β) and stabilizes Notch3, a protein implicated in non-small cell lung cancer. STRAP

More Related Videos

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
07:26

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis

Published on: April 1, 2022

Related Experiment Videos

Last Updated: Jun 2, 2026

Cell Aggregation Assays to Evaluate the Binding of the Drosophila Notch with Trans-Ligands and its Inhibition by Cis-Ligands
05:48

Cell Aggregation Assays to Evaluate the Binding of the Drosophila Notch with Trans-Ligands and its Inhibition by Cis-Ligands

Published on: January 2, 2018

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
07:26

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis

Published on: April 1, 2022

Area of Science:

  • Cellular signaling pathways
  • Protein-protein interactions
  • Cancer biology

Background:

  • Glycogen synthase kinase 3β (GSK3β) regulates cellular processes by phosphorylating substrates.
  • The recruitment mechanisms for many GSK3β substrates remain unclear.
  • Notch signaling is implicated in various cancers, including non-small cell lung cancer (NSCLC).

Purpose of the Study:

  • To elucidate the interaction between GSK3β and its novel scaffold protein, STRAP.
  • To investigate the role of STRAP in the regulation of Notch3 stability and function.
  • To explore the potential oncogenic role of STRAP in non-small cell lung cancer.

Main Methods:

  • Co-immunoprecipitation assays to establish protein binding.
  • Use of small-molecule inhibitors to probe protein interactions.
  • In vivo ubiquitination assays to assess protein stability.
  • Immunohistochemical staining of tissue microarrays for co-localization studies.

Main Results:

  • STRAP binds to GSK3β via its WD40 domains, forming a ternary complex with GSK3β and Axin.
  • STRAP binds to the intracellular fragment of Notch3 (ICN3) through its ankyrin repeat region.
  • STRAP reduces ICN3 ubiquitination, leading to ICN3 stabilization.
  • STRAP and Notch3 are co-upregulated and co-localized in a significant proportion of NSCLC tissues.

Conclusions:

  • STRAP acts as a scaffold protein that modulates GSK3β activity towards Notch3.
  • STRAP stabilizes ICN3, potentially contributing to its oncogenic functions in NSCLC.
  • The findings reveal a novel regulatory mechanism for Notch3 and highlight STRAP as a potential therapeutic target in NSCLC.