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Related Experiment Videos

The prion protein requires cholesterol for cell surface localization.

Sabine Gilch1, Claudia Kehler, Hermann M Schätzl

  • 1Institute of Virology, Technical University of Munich, Biedersteiner Str. 29, D-80802 Munich, Germany.

Molecular and Cellular Neurosciences
|November 10, 2005
PubMed
Summary

Cholesterol is vital for cell surface localization of the cellular prion protein (PrP(c)). Inhibiting cholesterol synthesis causes PrP(c) to accumulate in the Golgi, preventing its cell surface presence and prion conversion.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • The cellular prion protein (PrP(c)) is a cell surface protein associated with lipid rafts.
  • Lipid rafts are cholesterol-rich membrane microdomains crucial for PrP(c) function.
  • Cholesterol synthesis disruption affects prion conversion, suggesting a role in PrP(c) trafficking.

Purpose of the Study:

  • To investigate how inhibiting cholesterol synthesis impacts PrP(c) trafficking in neuronal cells.
  • To understand the role of cholesterol in PrP(c) localization and its implications for prion conversion.

Main Methods:

  • Neuronal cells were treated with mevinolin, an HMG-CoA-reductase inhibitor, to block cholesterol synthesis.
  • Cell surface PrP(c) levels were quantified.

Related Experiment Videos

  • PrP(c) localization within cellular compartments, including the Golgi, was analyzed using mutant PrPs.
  • The importance of the glycosyl-phosphatidyl-inositol (GPI) anchor for raft localization was examined.

    • Main Results:

    • Mevinolin treatment significantly reduced the amount of PrP(c) at the cell surface.
    • Inhibition of cholesterol synthesis led to PrP(c) accumulation within the Golgi apparatus.
    • Analysis of PrP mutants confirmed the GPI anchor's role in raft localization.
    • Specific domains involved in PrP raft association within the secretory pathway were identified.

    Conclusions:

    • Cholesterol is essential for maintaining PrP(c) at the cell surface.
    • Disruption of cholesterol synthesis impairs PrP(c) trafficking, leading to Golgi accumulation.
    • These findings underscore cholesterol's critical role in PrP(c) cell surface localization, a prerequisite for prion conversion.