Interaction of the Deubiquitinating Enzyme Ubp2 and the E3 Ligase Rsp5 Is Required for Transporter/Receptor Sorting in the Multivesicular Body Pathway
2009
Ubp2's Role in Protein Sorting in Yeast
publication
10 minutes
Evidence: moderate
Author Information
Author(s): Lam Mandy H. Y., Urban-Grimal Danièle, Bugnicourt Amandine, Greenblatt Jack F., Haguenauer-Tsapis Rosine, Emili Andrew
Primary Institution: University of Toronto
Hypothesis
Ubp2 modulates the sorting of membrane proteins in the multivesicular body pathway.
Conclusion
Ubp2 is a positive regulator of Rsp5-mediated membrane protein trafficking after endocytosis.
Supporting Evidence
- Ubp2 interacts with the E3 ligase Rsp5 and the protein Rup1.
- Deletion of UBP2 leads to stabilization of the Fur4 protein at the plasma membrane.
- Ubp2 is involved in the sorting of the uracil permease Fur4 in yeast.
Takeaway
Ubp2 helps proteins get sorted correctly inside yeast cells, which is important for their function.
Methodology
The study used yeast strains with specific gene deletions and performed experiments to analyze protein interactions and trafficking.
Limitations
The study primarily focuses on yeast and may not directly translate to other organisms.
Digital Object Identifier (DOI)
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