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Non-Canonical Wnt Signaling Pathways01:41

Non-Canonical Wnt Signaling Pathways

Wnt is a zygotic effect gene that is expressed during very early embryonic development. It regulates various processes in animals starting from early development through the adult stage, such as organogenesis in the embryo and maintenance of neuronal and blood stem cells. Wnt proteins can induce a wide variety of intracellular pathways depending upon the specific abilities of different Wnt ligands to form a complex with shared and cognate receptors in the presence of different co-receptors. The...
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The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
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Updated: May 21, 2026

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Structural basis of the interaction between Norrin-Tspan12.

Lulu Xue1, Min Zhang1, Zhizhuo Dai1

  • 1School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.

Structure (London, England : 1993)
|May 19, 2026
PubMed
Summary
This summary is machine-generated.

Tetraspanin 12 (Tspan12) binds Norrin, a Wnt ligand, revealing a structural basis for Norrin signaling. This interaction is crucial for understanding familial exudative vitreoretinopathy (FEVR) and developing targeted therapies.

Keywords:
Cryo-EMFEVRNorrinTspan12

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Signaling

Background:

  • Norrin, an atypical Wnt ligand, activates beta-catenin signaling via Frizzled 4 (FZD4), LRP5/6 co-receptors, and Tetraspanin 12 (Tspan12).
  • The precise mechanism of Tspan12's role in Norrin signaling has been elusive.
  • Mutations in these components are linked to familial exudative vitreoretinopathy (FEVR).

Purpose of the Study:

  • To elucidate the molecular mechanism of Tspan12's enhancement of Norrin signaling.
  • To determine the structural basis of the Norrin-Tspan12 interaction.
  • To provide insights into FEVR pathogenesis and therapeutic strategies.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of the Norrin-Tspan12 LEL complex.
  • Biochemical assays to assess binding affinities.
  • Structural analysis to define the interaction interface.

Main Results:

  • The cryo-EM structure of the Norrin-Tspan12 LEL complex was determined at 3.78 Å resolution.
  • A Norrin dimer was observed to bind two Tspan12 molecules, defining the interaction interface.
  • Tspan12 directly binds Norrin without altering Norrin's affinity for FZD4, supporting a quaternary complex model.

Conclusions:

  • The study reveals the structural basis for Tspan12's interaction with Norrin.
  • Findings support a model where Norrin, FZD4, LRP5/6, and Tspan12 form a quaternary signaling complex.
  • These insights are critical for understanding FEVR and developing targeted therapies.