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Notch Signaling Pathway03:14

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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.
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Related Experiment Video

Updated: Mar 6, 2026

Cell Aggregation Assays to Evaluate the Binding of the Drosophila Notch with Trans-Ligands and its Inhibition by Cis-Ligands
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Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity.

Vincent C Luca1,2, Byoung Choul Kim3,4, Chenghao Ge5

  • 1Departments of Molecular and Cellular Physiology and Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.

Science (New York, N.Y.)
|March 4, 2017
PubMed
Summary
This summary is machine-generated.

Notch receptor activation relies on mechanical force and glycosylation. New structural data reveals how Jagged1 binding to Notch1 uses these forces to regulate cell fate decisions.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Notch signaling is crucial for cell fate determination.
  • This pathway is unique in its dependence on mechanical forces and protein glycosylation.
  • Understanding the molecular interactions is key to deciphering Notch pathway regulation.

Purpose of the Study:

  • To elucidate the structural basis of Notch1 and Jagged1 (Jag1) interaction.
  • To investigate the role of mechanical force and glycosylation in Notch1-Jag1 binding.
  • To compare Notch1 binding to Jag1 versus Delta-like 4 (DLL4) ligands.

Main Methods:

  • X-ray crystallography at 2.5-angstrom resolution.
  • Analysis of protein-protein binding interfaces.
  • Characterization of protein glycosylation modifications (O-linked fucose).

Main Results:

  • A detailed structure of the Notch1-Jag1 extracellular complex was determined.
  • O-linked fucose on Notch1 EGF domains 8 and 12 interacts with Jag1 EGF3 and C2 domains.
  • Jag1 exhibits catch bond behavior upon Notch1 binding, influenced by mechanical forces.
  • Notch1 utilizes different domains for Jag1 binding compared to DLL4 binding.

Conclusions:

  • Mechanical forces and specific glycosylation patterns are critical for Notch1-Jag1 interaction.
  • Jag1's catch bond behavior allows force-dependent regulation of Notch signaling.
  • This provides a mechanism for ligand discrimination and potentiation of Notch signaling through mechanical cues.