Decoding ubiquitin chain signals in physiologic and stressed states

Although Lys48-linked ubiquitin is the canonical signal for protein clearance by the proteasome, ‘alternative’ ubiquitin signals play critical yet poorly-characterised roles in misfolded protein clearance—especially under acute stress. Using linkage-specific ubiquitin probes and perturbation tools, we are uncovering how these additional ubiquitin signalling events maintain proteome robustness in a range of physiologic and stressed cellular contexts.

Current projects on ubiquitin signalling include:

Impact of specific ubiquitin linkages in misfolded protein clearance

• Project Leads: Harvey Johnston; Richard Odle
• Collaborators: Yogesh Kulathu; Helle Ulrich; Gabriele Kaminski-Schierle; Kirby Swatek

Nascent proteome quality control during dendritic cell activation

• Project Lead: Estelle Wu
• Co-PI: Michelle Linterman
• Collaborators: Ed Roberts