Screen for ISG15-crossreactive Deubiquitinases
Author Information
Author(s): Catic André, Fiebiger Edda, Korbel Gregory A., Blom Daniël, Galardy Paul J., Ploegh Hidde L.
Primary Institution: Harvard Medical School
Hypothesis
Promiscuous deubiquitinating proteases (DUBs) might exist, capable of recognizing both ubiquitin and ISG15.
Conclusion
ISG15 utilizes both the conjugating and deconjugating machinery of ubiquitin, indicating a more extensive functional overlap than previously appreciated.
Supporting Evidence
- 22 human DUBs were cloned and expressed.
- USP2, USP5, USP13, and USP14 were identified as ISG15-reactive proteases.
- USP14's activity increases when complexed with the proteasome.
Takeaway
Scientists found that some proteins can recognize and work with both ubiquitin and ISG15, which are similar molecules in the body.
Methodology
Cloned and expressed 22 human DUBs and identified ISG15-reactive proteases using activity-based profiling.
Limitations
The study does not identify all potential ISG15-specific proteases and relies on specific experimental conditions.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website