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Confocal Microscopy Reveals Cell Surface Receptor Aggregation Through Image Correlation Spectroscopy
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EGFR Aggregation in the Brain.

Omid Tavassoly1, Iman Tavassoly2

  • 1Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.

ACS Chemical Neuroscience
|May 12, 2021
PubMed
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Preformed fibrils of misfolded proteins like alpha-synuclein and amyloid-beta activate the epidermal growth factor receptor (EGFR), promoting amyloid aggregation and propagation in cells and animal models.

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Amyloidogenic domainEGFRneurodegenerationreceptor aggregation

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Misfolded proteins, such as alpha-synuclein (α-syn) and amyloid-beta (Aβ), form preformed fibrils (PFFs) implicated in neurodegenerative diseases.
  • Epidermal growth factor receptor (EGFR) is a key cell surface receptor involved in cell growth and survival.
  • Amyloid propagation involves the spread of misfolded protein aggregates.

Purpose of the Study:

  • To investigate the role of EGFR in the activation and propagation of misfolded protein fibrils.
  • To explore the mechanism by which PFFs interact with EGFR.
  • To determine if EGFR acts as an amyloidogenic receptor.

Main Methods:

  • Cell culture experiments to observe EGFR activation by PFFs.
  • Animal models of amyloid propagation were utilized.
  • Comparison of PFFs' effects with known EGFR ligands (EGF, HB-EGF).

Main Results:

  • Preformed fibrils (PFFs) of α-synuclein and Aβ were shown to activate EGFR.
  • EGFR activation by PFFs leads to high-order clustering and aggregation of the EGFR tyrosine kinase domain (EGFR-TKD).
  • Self-assembled EGFR-TKD fibrils can seed the aggregation of endogenous misfolded proteins.

Conclusions:

  • EGFR acts as an amyloidogenic receptor, facilitating the uptake of exogenous PFFs.
  • EGFR signaling contributes to the seeding and propagation of endogenous misfolded proteins.
  • This mechanism highlights a novel pathway in amyloid diseases involving EGFR-mediated aggregation.