Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Andreas Damianou and Hannah Jones from the Kessler lab, together with the DisPro team, tackle the long-standing challenge of identifying direct deubiquitinase (DUB) substrates by combining APEX2-based proximity labeling with K-ε-GG ubiquitin remnant enrichment. This proximal-ubiquitomics approach enables site-specific, spatially resolved detection of deubiquitination events.

Graphical abstract - USP30

Using the mitochondrial DUB USP30 as a case study, we recovered known substrates (TOMM20, FKBP8) and identified LETM1 as a novel USP30-regulated substrate. This method offers a valuable framework for dissecting DUB- and also E3-substrate interactions in native cellular contexts. Read the full article here.