Weaponizing Ubiquitin to Target Ubiquitin-C Terminal Hydrolase L1

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Researchers at Purdue University have developed a ubiquitin protein mutant that will selectively bind Ubiquitin C-Terminal Hydrolase L1 (UCHL1) enzyme over all other deubiquitinating enzymes (DUBs) expressed in cells. The ubiquitination process involves adding the ubiquitin protein to substrate proteins. This protein conjugation event can have different cellular effects on the substrate protein depending on the location and length of the ubiquitin linkages. DUBs are proteins that are responsible for cleaving ubiquitin linkages to maintain ubiquitin levels in the cell. One such enzyme, UCHL1, is overexpressed in a multitude of aggressive cancers and is involved with neurological diseases like Parkinson's disease and Alzheimer's disease. However, the specific role UCHL1 plays in these disease states remains enigmatic. Researchers at Purdue University have developed a macromolecular ubiquitin mutant for probing UCHL1's activity in a cellular environment. This technology offers a novel approach to studying UCHL1's role in certain disease states by probing intracellular UCHL1 activity in real time, a feat that has not been accomplished with any deubiquitinating enzyme. Also, this technology can be repurposed to provide a covalent macromolecular inhibitor of UCHL1, providing another layer of novelty to UCHL1 activity studies.

-UCHL1 Selective Probe
-Real Time UCHL1 Activity Assay
-Multi-Disease Relevance

Potential Applications:
-Probe Intracellular UCHL1
Aug 12, 2020
United States
Purdue Office of Technology Commercialization
The Convergence Center
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West Lafayette, IN 47906

Phone: (765) 588-3475
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Email: otcip@prf.org