How Glycosylation Affects Prion Protein Sorting
Author Information
Author(s): Puig Berta, Altmeppen Hermann C., Thurm Dana, Geissen Markus, Conrad Catharina, Braulke Thomas, Glatzel Markus
Primary Institution: Institute of Neuropathology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany
Hypothesis
The study investigates the role of N-glycans and the GPI-anchor in the polarized sorting of mouse PrPC in MDCK cells.
Conclusion
Both N-glycosylation and GPI-anchor influence the polarized sorting of PrPC, with the GPI-anchor being the dominant factor.
Supporting Evidence
- The study found that lack of one N-linked oligosaccharide leads to loss of polarized sorting of PrPC.
- Replacing the GPI-anchor of PrPC with that of Thy-1 redirects PrPC to the apical membrane.
- Confocal microscopy showed that PrPC mutants were present at both apical and basolateral membranes.
Takeaway
This study shows that the way a protein is modified can change where it goes in a cell, which is important for understanding diseases like prion diseases.
Methodology
The study involved mutating N-glycosylation sites and GPI-anchor of PrPC and analyzing their effects on protein sorting using confocal microscopy and biotinylation assays.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website