An important role for the ubiquitin system is in the quality control and degradation 
of misfolded and damaged proteins, a process central to maintaining proteostasis. Ubiquitylation also has important non-degradative roles in signalling pathways. One of the ways ubiquitylation is able to mediate such a diverse array of functions is because a range of different ubiquitin signals can be formed. How does the cellular machinery distinguish between different ubiquitin signals to orchestrate a specific response? And what regulatory mechanisms ensure that ubiquitin signals are tightly regulated?

Our lab is interested in understanding (i) how ubiquitylation regulates protein degradation and proteostasis, and (ii) how ubiquitin signalling regulates T-lymphocyte biology and immune responses. To address these fundamental questions, we combine structural, biochemical and genetic approaches to uncover and understand the underlying pathways and mechanisms.

Our research has provided insights into the assembly and recognition of different ubiquitin signals. We recently discovered novel regulators of protein degradation that are highly conserved in evolution. Failure to degrade proteins in a timely manner is the underlying cause 
of diseases such as cancer and neurodegeneration. By studying
 how ubiquitylation regulates protein degradation and proteostasis we hope to better understand the molecular causes of disease that we can exploit for the development of effective therapeutic strategies.