Dr Ruth Densham PhD M.Biochem (Hons)

Dr Ruth Densham

Institute of Cancer and Genomic Sciences
Senior Postdoctoral Fellow

Contact details

IBR West Level 1
Institute of Cancer and Genomic Sciences
University of Birmingham
B15 2TT

Ruth is interested in understanding the complex signalling events that control how a cell senses and repairs DNA damage in order to maintain genome integrity. She has a special interest in the roles of the breast and ovarian cancer predisposition protein, BRCA1, and its partner protein BARD1 in DNA repair and how post-translational modifications influence these processes. 

Ruth has published a growing number of primary papers and reviews in scientific journals. In addition, she has co-authored a book chapter on “Ubiquitin and Sumo in the DNA damage response” for a new textbook on DNA repair and replication.


  • PhD in Cell Signalling, The Babraham Institute & University of Cambridge, 2005
  • M.Biochem, University of Bath, 2001


Ruth studied Biochemistry as an undergraduate at the University of Bath and qualified with an M.Biochem in 2001. She went on to study for a PhD in Cell Signalling with Dr Simon Cook at the Babraham Institute, before graduating from the University of Cambridge in 2005. 

In 2005, Ruth moved to the Beatson Institute in Glasgow to work with Professor Michael Olson where she studied how the cell senses and responds to cytoskeletal stress. 

In 2008, Ruth joined Professor Jo Morris at King’s College London to work on BRCA1 SUMOylation and the DNA damage response before moving with Jo to the University of Birmingham in 2010. Ruth is currently a Senior Research Fellow with Professor Jo Morris in the Institute of Cancer and Genomic Sciences and continues to study the role of the BRCA1-BARD1 complex in DNA repair. 


Ruth teaches on the following modules for BSc Biomedical Science:

Year 1

  • Transition to University
  • Introduction to Experimental Design 

Year 2

  • Cancer and Stratified Medicine
  • Stem Cells and Genetic Inheritance

 Year 3  

  •  New Targets and Drugs in Cancer Therapy (co-module Lead)


The Morris lab has recently shown that the BRCA1 ligase activity is required for a subset of DNA damage responses by using novel separation of function mutations in BRCA1’s binding partner BARD1 that specifically impair ligase activity. BRCA1-BARD1 ligase activity is required for C-terminal H2A-Ubiquitination and this ubiquitin mark promotes long range resection, required for accurate homology-directed repair, via the activity of the Chromatin Remodeller, SMARCAD1. 

This work has been extended by our identification of the de-ubiquitinating enzyme, USP48, which specifically deubiquitinases the BRCA1-BARD1 H2A-Ub mark. USP48 activity acts to restrain resection length and control homology-directed repair pathway choice. Hyper-resection occurs in the absence of USP48 due to the uncontrolled spread of the BRCA1-BARD1 H2A-Ub modification and this promotes both gene conversion and the mutagenic single strand annealing pathway. Therefore, we propose a model in which USP48 protects genome integrity by controlling resection lengths.    

We are interested in manipulating the BRCA1-BARD1-H2Aub-SMARCAD1-USP48 pathway to better understand the complexities of DNA repair. In addition, we are seeking to understand the effects of patient variants found in these genes and their relationship to cancer predisposition.

Ruth is a Senior Research Fellow with Professor Jo Morris.

Ruth is part of the Birmingham Centre for Genome Biology and also works with Colleagues at the School of Chemistry.   

Ruth also collaborates with researchers at the NKI in the Netherlands and with researchers at the University of Nottingham


Spiliotopoulos A, Blokpoel Ferreras L, Densham RM, Caulton SG, Maddison BC, Morris JR, Dixon JE, Gough KC, Dreveny I. Discovery of peptide ligands targeting a specific ubiquitin-like domain-binding site in the deubiquitinase USP11. J Biol Chem. (2018) pii: jbc.RA118.004469. doi: 10.1074/jbc.RA118.004469. 

Densham, RM, Garvin, AJ & Morris, JR.Ubiquitin, SUMO and the DNA double strand break response.  In book: DNA Repair and Replication: Mechanisms and Clinical Significance Publisher: Garland Science; 1 edition (5 Sept. 2018)   doi: 10.1201/9780429464744-9 

Uckelmann M*, Densham RM*, Winterwerp HHK, Fish A, Sixma TK, Morris JR. USP48 restrains resection by site specific cleavage of the BRCA1 ubiquitin mark from H2A. Nature Communications  (2018) 9:229  *joint first authors doi: 10.1038/s41467-017-02653-3 

Densham RM, Morris JR. The BRCA1 Ubiquitin ligase function sets a new trend for remodelling in DNA repair. Nucleus. (2016) 29:1-10. doi: 10.1080/19491034.2016.1267092.

Densham RM, Garvin AJ, Stone HR, Strachan J, Baldock RA, Daza-Martin M, Fletcher A, Blair-Reid SA, Beesley J, Johal B, Pearl LH, Neely R, Keep NH, Watts FZ, Morris JR. Human BRCA1-BARD1 Ubiquitin ligase activity counters chromatin barriers to DNA resection. Nature Struc. Mol. Biol. (2016)  23 647-655 doi:10.1038/nsmb.3236

Garvin AJ, Densham RM, Blair-Reid SA, Pratt KM, Stone RM, Weekes D, Lawrence KJ, and Morris JR. The deSUMOylase SENP7 promotes chromatin relaxation for homologous recombination DNA repair. EMBO reports (2013) 14(11) 975-83. doi: 10.1038/embor.2013.141.

Butler LR, Densham RM, Jia J, Garvin AJ, Stone HR, Shah V, Weekes D, Festy F, Beesley J, Morris JR. The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response. EMBO J. (2012) 31(19) 3918-34. doi: 10.1038/emboj.2012.232.

Morris JR, Boutell C, Keppler M, Densham R, Weekes D, Alamshah A, Butler L, Galanty Y, Pangon L, Kiuchi T, Ng T, Solomon E. The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress. Nature. (2009) 462 (7275) 886-90. doi: 10.1038/nature08593

Densham RM, O'Neill E, Munro J, König I, Anderson K, Kolch W, Olson MF. MST kinases monitor actin cytoskeletal integrity and signal via c-Jun N-terminal kinase stress-activated kinase to regulate p21Waf1/Cip1 stability. Mol Cell Biol. (2009) 29 (24) 6380-90. doi: 10.1128/MCB.00116-09

Densham RM, Todd DE, Balmanno K, Cook SJ. ERK1/2 and p38 cooperate to delay progression through G1 by promoting cyclin D1 protein turnover. Cell Signal. (2008) 20 (11) 1986-94. doi: 10.1016/j.cellsig.2008.07.005  

Coleman ML, Densham RM, Croft DR, Olson MF. Stability of p21Waf1/Cip1 CDK inhibitor protein is responsive to RhoA-mediated regulation of the actin cytoskeleton. Oncogene. (2006) 252708-16.   

Todd DE, Densham RM, Molton SM, Balmanno K, Newson C, Weston CR, Garner AP, Scott L, Cook SJ.  ERK1/2 and p38 cooperate to induce a p21Cip1-dependent G1 cell cycle arrest.  Oncogene (2004) 23 3284-3295

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