Dr Mathew Coleman BSc, PhD

Dr Mathew Coleman

Institute of Cancer and Genomic Sciences
Senior Lecturer

Contact details

Address
Institute of Cancer and Genomic Sciences
College of Medical and Dental Sciences
University of Birmingham
Edgbaston
Birmingham
B15 2TT
UK

Mathew Coleman is a Senior Lecturer in the Institute of Cancer and Genomic Sciences, where his research focusses on the role of protein hydroxylation in the cell biology of tumour cells.

Mathew has attracted highly competitive funding support from Cancer Research UK, the MRC, BBSRC and Glaxo Smith Kline. His work on protein hydroxylation has led to patents, and highly cited articles and high impact research and review publications including most recently in Nature, Nature Chemical Biology, PNAS and Molecular Cell.

Qualifications

  • PhD in Tumour Cell Biology, 2002 (Institute of Cancer Research, London)
  • BSc in Medical Biochemisty, 1998 (Brunel University, London)

Biography

Mathew Coleman qualified with a first class honours from Brunel University in 1998 before undertaking a PhD at the Institute of Cancer Research with Professor Christopher Marshall and Dr Michael Olson. His PhD work focussed on the role of Ras and Rho GTPase signalling pathways in cell proliferation and apoptosis and led to review and research articles in EMBO, Nature Reviews Molecular and Cellular Biology, and Nature Cell Biology. The latter article describing the mechanism of apoptotic membrane blebbing has attracted more than 700 citations.

Following his PhD Mathew undertook a post-doctoral position at the Abramson Family Cancer Research Institute (Philadelphia, USA) working on the B-Raf V600E oncogene before returning to the UK in 2004 to work with Professor Sir Peter Ratcliffe at the University of Oxford. With support from a Jesus College Junior Research Fellowship Mathew explored his interests in novel post-translational modifications, discovering several new substrates for protein hydroxylases involved in hypoxia signalling. During this time he published research articles in The Journal of Biological Chemistry, The Biochemical Journal, PNAS, and review articles in Essays in Biochemistry and Nature Medicine.

In 2009 a Fellowship jointly funded by the OAK foundation and the Nuffield Department of Medicine (Oxford) supported him in studying cancer-associated protein hydroxylases. Together with Professor Christopher Schofield (Chemistry department, Oxford University) he demonstrated for the first time that the ribosome is a novel target of protein hydroxylases (Ge et al, Nature Chemical Biology, 2012). With an MRC New Investigator Award Mathew established his independent research laboratory in the Institute of Cancer and Genomics Sciences at the University of Birmingham in 2013. There his group were the first to report the regulation of translational termination by lysyl hydroxylation (Feng et al, Molecular Cell, 2014). The Coleman group continues to explore the role of protein hydroxylation in physiology and disease.

Teaching

Postgraduate supervision

Mathew has supervised three students to successful completion of their PhDs. His third student first authored papers published in Nature Chemical Biology and Molecular Cell. His fourth PhD student is currently studying the role of protein hydroxylases in cancer, and is funded by a prestigious GSK/BBSRC studentship that provides 6 months industrial experience in the USA. Mathew is currently supervising two other PhD students, and has successfully mentored a variety of MSc and undergraduate students and interns.

The Tumour Oxygenase Group always welcomes applications from talented and enthusiastic students to study the role of protein hydroxylation in cancer. For this and related doctoral research enquiries, please contact Mathew on the details above.

Alternatively, email: dr@contacts.bham.ac.uk or call +44 (0)121 414 5005.

For a full list of available Doctoral Research opportunities, please visit our Doctoral Research programme listings.

Research

The Tumour Oxygenase Group is currently investigating the molecular mechanisms by which protein hydroxylases that are amplified, mutated or deleted in specific cancer types contribute to tumourigenesis. To do this we take a multi-disciplinary approach that includes:

  1. Biochemistry: recombinant protein expression, in vitro enzyme and interaction assays.
  2. Functional genomics: RNA interference to identify protein hydroxylases with specific loss-of-function phenotypes in tumour cells.
  3. Substrate discovery: Immunopurification of epitope-tagged hydroxylases and identification of associated substrates by mass spectrometry.
  4. Tumour cell biology: protein and RNA quantitation, protein:protein interactions, cell growth and apoptosis assays, hypoxia and inhibitor treatments.
  5. Cancer genetics: Bioinformatics to identify altered hydroxylases in cancer, genomic DNA sequencing of tumour samples.
  6. Pathology: Detection of hydroxylases and substrates in tumour samples by immunohistochemistry.Cell transformation and tumour models.

Publications

Ploumakis A and Coleman ML, 2015. OH, the Places You’ll Go! Hydroxylation, Gene expression and Cancer. Molecular Cell. 58 (5), 729-41

Zhuang QQ, Feng T, and Coleman ML, 2015. Modifying the maker: Oxygenases target ribosome biology. Translation. 3 (1), e1009331

Singleton RS, Liu-Yi P, Formenti F, Ge W, Sekirnik R, Fischer R, Adam J, Pollard PJ, Wolf A, Thalhammer A, Loenarz C, Flashman E, Yamamoto A, Coleman ML, Kessler BM, Wappner P, Schofield CJ, Ratcliffe PJ, Cockman ME. 2014, OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation. PNAS, 111(11):4031-6.

Tianshu Feng, Atsushi Yamamoto, Sarah E. Wilkins, Elizaveta Sokolova, Luke A. Yates,Martin Münzel, Pooja Singh, Richard J. Hopkinson, Roman Fischer, Matthew E. Cockman, Jake Shelley, David C. Trudgian, Johannes Schödel, James S. O. McCullagh, Wei Ge, Benedikt M. Kessler, Robert J. Gilbert, Ludmila Y. Frolova, Elena Alkalaeva, Peter J. Ratcliffe, Christopher J. Schofield, and Mathew L. Coleman, 2014, Optimal Translational Termination Requires C-4 Lysyl Hydroxylation of eRF1, Molecular Cell, 53(4), 645-54. Front Cover.

Yosef N, Shalek AK, Gaublomme JT, Jin H , Lee Y, Awasthi A, Wu C, Karwacz K, Xiao S, Jorgolli M, Gennert D, Satija R, Shakya A, Lu DY, Trombetta JJ, Pillai MR, Ratcliffe PJ, Coleman ML, Bix M, Tantin D, Park H, Kuchroo VK, Regev A, 2013, Dynamic regulatory network controlling Th17 cell differentiation, Nature, 496, 461-468.

Ge W, Wolf A, Feng T, Ho CH, Sekirnik R, Zayer A, Granatino N, Cockman ME, Loenarz C, Loik ND, Hardy AP, Claridge TD, Hamed RB, Chowdhury R, Gong L, Robinson CV, Trudgian DC, Jiang M, Mackeen MM, McCullagh JS, Gordiyenko Y, Thalhammer A, Yamamoto A, Yang M, Liu-Yi P, Zhang Z, Schmidt-Zachmann M, Kessler BM, Ratcliffe PJ, Preston GM, Coleman ML*, Schofield CJ*, 2012, Oxygenase catalysed ribosome hydroxylation is conserved from prokaryotes to humans, Nature Chemical Biology, 8, 960-962. *Equal contribution and corresponding author.

Yang M, Ge W, Chowdhury R, Claridge TD, Kramer HB, McDonough MA, Kessler BM, Ratcliffe PJ, Coleman ML*, Schofield CJ*, 2011, Asparaginyl and aspartyl hydroxylation of the cytoskeletal ankyrin family is catalysed by factor inhibiting hypoxia-inducible factor (FIH), J Biol Chem, 286, 7648-60. *contributed equally.

Loenarz C, Coleman ML, Boleininger A, Schierwater B, Holland PW, Ratcliffe PJ, Schofield CJ, 2011, The hypoxia-inducible transcription factor pathway regulates oxygen sensing in the simplest animal, Trichoplax adhaerens, EMBO Rep,12, 63-70.

Brady SC, Coleman ML, Munro J, Feller SM, Morrice NA, Olson MF, 2009, Sprouty2 association with B-Raf is regulated by phosphorylation and kinase conformation, Cancer Res, 69, 6773-81.

Coleman ML* and Ratcliffe PJ, 2009, Signalling Cross Talk of the HIF System: Involvement of the FIH Protein, Curr Pharm Des, 15, 3904-7. *corresponding author.

Coleman ML, Ratcliffe PJ, 2009, Angiogenesis: escape from hypoxia. Nature Medicine, 15, 491-3.Webb JD, Murányi A, Pugh CW, Ratcliffe PJ, and Coleman ML, 2009, MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting