Kathryn S. Lilley

Kathryn S. Lilley

Talk Title: The dynamics of the spatial proteome.


Kathryn received her PhD in Biochemistry from the University of Sheffield in 1990. She continued her scientific career as a laboratory manager for 11 years at the University of Leicester where she ran the Protein and Nucleic Acid Laboratory core facility. In November 2000, she established the Cambridge Center for Proteomics (CCP) of which she is director which sits within the Cambridge Systems Biology Centre, University of Cambridge. This state-of-the-art center collaborates with a large number of groups in the UK and worldwide.
In parallel to this, she established a research programme and her laboratory is now at the forefront of technology development which enables measurement of the dynamics of the proteome in a high throughput manner in space and time during critical cellular processes such as signaling and differentiation. Her group has also contributed many open-source informatics tools necessary to efficiently mine and visualize the extremely complex data which is produced by spatiotemporal proteomics studies.
She was appointed to a Professorship in Cellular Dynamics in 2012 and more recently has been awarded a Welcome Trust Investigator Award to investigate the implication of where transcripts are translated upon the spatial proteome and how this process is controlled.

Abstract: What controls the three dimensional proteome?

Kathryn Lilley, Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB1 3QL

Proteins can adopt multiple functions, depending on the isoform expressed, and variations in their sub-cellular location, binding partners and post-translational modifications. Such differential control significantly increases the functionality of the proteome. The processes governing these features are highly dynamic and their aberrant control is implicated in many diseases.
We have developed methods to determine the three dimensional organisation of the proteome in eukaryote cells in a single experiment with high resolution (Mulvey et al, Nature Protocols (2017)). We have applied this method to many different biological systems, including mapping protein relocalization upon perturbation. Intriguingly, we consistently observe that up to half the proteome cannot be discretely assigned to a single localisation. This observation has been recently supported by comparing two very different approaches to map proteins to their subcellular niches (Thul et al, Science (2017)).
In this presentation I will discuss factors controlling protein location and the interplay of the metabolism and signalling mechanisms on the spatial proteome.