Simon Walker

Simon Walker
Simon Walker
Simon Walker
Head of Imaging Facility
Simon Walker

Simon has a BSc in Biochemistry from Hertiot-Watt University (Edinburgh) and a PhD from the University of East Anglia (Norwich). Simon studied for his PhD at the John Innes Centre in Norwich under the supervision of Prof. J. Allan Downie, investigating the role of calcium signalling during legume symbiosis. It was during this time that Simon first used a confocal microscope, sparking an interest in microscopy and imaging technology.

Following his PhD, Simon went to work as a postdoc in Pete Cullen's lab in the Department of Biochemistry at Bristol University, investigating Ras GTPase-activating proteins. These studies required the use of various microscopy systems and cemented Simon’s passion for biological imaging. Simon moved to the Babraham Institute in 2004 where he established the Institute’s core Imaging Facility.

The Imaging Facility now provides state-of-the-art microscopy services essential for the delivery of Institute science and is an important Babraham Research Campus resource supporting the commercial research community.

Latest Publications

Kara N, Biggins L, Whale A, May K, Grinkevich V, Garran-Garcia P, Srinivasan J, Rugg-Gunn PJ, de Almeida CR, Walker SJ, Picco G, Garnett MJ, Andrews S, Parry A, Robinson HMR, Houseley J Epigenetics , Genomics , Biological Support Unit , Bioinformatics

TrAEL-seq is a robust method for profiling DNA replication genome-wide that works in unsynchronized cells and does not require drugs or nucleotide analogues. Here, we provide an updated method for TrAEL-seq that improves sample quality and includes multiplexing of up to six samples which dramatically improves throughput, and we validate TrAEL-seq in multiple mammalian cell lines. The updated protocol is straightforward and robust yet provides excellent resolution comparable to OK-seq in mammalian cell samples. High resolution replication profiles can be obtained across large panels of samples and in dynamic systems, for example during the progressive onset of oncogene induced senescence. In addition to mapping zones where replication initiates and terminates, TrAEL-seq is sensitive to replication fork speed, revealing effects of both transcription and proximity to replication Initiation Zones on fork progression. Although forks move more slowly through transcribed regions, this does not have a significant impact on the broader dynamics of replication fork progression, and instead replication forks accelerate across the first ∼1 Mb of travel irrespective of local transcriptional activity. We propose that this is a consequence of fewer replication forks being active later in S-phase when these distal regions replicate and there being less competition for replication factors.

+view abstract Nucleic acids research, PMID: 41830325

Molina ISM, Okkenhaug H, Walker S, Linterman M, Marcial-Juárez E

We developed a 50-plex imaging protocol using the MACSima platform to characterize the microarchitecture of germinal centers in secondary lymphoid tissues. This workflow combines tissue processing, automated cyclic imaging, image preprocessing, and a new analysis method that detects morphological changes in irregularly shaped stromal cells.

+view abstract European journal of immunology, PMID: 41732996

Bertran MT, Walmsley R, Cummings T, Aramburu IV, Benton DJ, Mora Molina R, Assalaarachchi J, Chasampalioti M, Swanton T, Joshi D, Federico S, Okkenhaug H, Yu L, Oxley D, Walker S, Papayannopoulos V, Suga H, Christophorou MA, Walport LJ Epigenetics

Peptidylarginine deiminase IV (PADI4, PAD4) deregulation promotes the development of autoimmunity, cancer, atherosclerosis and age-related tissue fibrosis. PADI4 additionally mediates immune responses and cellular reprogramming, although the full extent of its physiological roles is unexplored. Despite detailed molecular knowledge of PADI4 activation in vitro, we lack understanding of its regulation within cells, largely due to a lack of appropriate systems and tools. Here, we develop and apply a set of potent and selective PADI4 modulators. Using the mRNA-display-based RaPID system, we screen >10 cyclic peptides for high-affinity, conformation-selective binders. We report PADI4_3, a cell-active inhibitor specific for the active conformation of PADI4; PADI4_7, an inert binder, which we functionalise for the isolation and study of cellular PADI4; and PADI4_11, a cell-active PADI4 activator. Structural studies with PADI4_11 reveal an allosteric binding mode that may reflect the mechanism that promotes cellular PADI4 activation. This work contributes to our understanding of PADI4 regulation and provides a toolkit for the study and modulation of PADI4 across (patho)physiological contexts.

+view abstract Nature communications, PMID: 39528459

Group Members

Simon Walker

Head of Imaging Facility

Anneliese Jarman

Image Analyst

Kirsty MacLellan-Gibson

Deputy Facility Manager & Senior EM Specialist

Isabel San Martin Molina

Imaging Specialist