How Rad23 Proteins Help Deliver Ubiquitinated Proteins to the Proteasome
Author Information
Author(s): Goh Amanda M, Walters Kylie J, Elsasser Suzanne, Verma Rati, Deshaies Raymond J, Finley Daniel, Howley Peter M
Primary Institution: Harvard Medical School
Hypothesis
The interactions between the UBL and UBA domains of Rad23 proteins modulate ubiquitin recognition and the delivery of ubiquitinated proteins to the proteasome.
Conclusion
The competition of ubiquitin-proteasome pathway components for surfaces on Rad23 is important for the role of the Rad23 family proteins in proteasomal targeting.
Supporting Evidence
- Disrupting the UBL-UBA interactions in Rad23 enhances its ability to bind ubiquitin.
- Mutations in the UBL domain affect Rad23's ability to deliver ubiquitinated proteins to the proteasome.
- The study shows that UBL-UBA interactions are crucial for Rad23's function in the ubiquitin-proteasome pathway.
Takeaway
Rad23 proteins help move tagged proteins to the garbage disposal of the cell, called the proteasome, by using special parts that grab onto these tagged proteins.
Methodology
The study involved mutating specific residues in the UBL domain of Rad23 and testing their effects on binding to ubiquitin and the proteasome using various biochemical assays.
Digital Object Identifier (DOI)
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