5:38 PM
 | 
Aug 08, 2018
 |  BC Innovations  |  Translation in Brief

Identifying the ubiquitinators

How a U.K. team is using mass spectrometry to identify ubiquitinating enzymes and their inhibitors

A team at University of Dundee and Newcastle University has developed a mass spectrometry-based screening platform to identify ubiquitin ligases and compounds that modulate them. The approach uses the uptake of ubiquitin by enzymes rather than chemical or fluorescent probes and could accelerate the screening of therapies that target the ubiquitin pathway.

Dysregulation of the ubiquitination pathway or mutations lead to aberrant protein levels in cells and are associated with several diseases including cancer, neurodegenerative disorders and immunological diseases.

Human cells degrade proteins via a ubiquitinating system comprising three classes of enzymes: E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes and E3 ubiquitin ligases. The E1 enzymes load ubiquitin onto the E2 enzymes, which then carry their cargo to specific proteins as directed by an E3 ubiquitin...

Read the full 604 word article

User Sign in

Trial Subscription

Get a 4-week free trial subscription to BioCentury Innovations

Article Purchase

$85 USD
More Info >