Investigating the essential roles of Ubiquitin-like molecules and the Ubiquitin Proteasome System

Ronald T. Hay


  • 1979: PhD in Virology Institute of Virology, University of Glasgow, UK.
  • 1975: BSc in Biochemistry, Heriot-Watt University, Edinburgh, UK.

Research Appointments

  • 2008: Honorary member Scottish Institute for Cell Signaling (SCILLS), University of Dundee.
  • 2005: Professor of Molecular Biology in the College of Life Sciences, Wellcome Trust Centre for Gene Regulation and Expression, University of Dundee.
  • 1985: Lecturer, Reader and Professor of Molecular Biology in the School of Biology, University of St Andrews.
  • 1982: Member of the scientific staff of the Medical Research Council Virology Unit, Institute of Virology, University of Glasgow.
  • 1979: Damon Runyon-Walter Winchell Cancer Fund Postdoctoral Fellow, Department of Biological Chemistry, Harvard Medical School, Boston, U.S.A..
Ronald T. Hay

Research Interests

  • Establishing the role of SUMO modification in the response of cells to DNA damage.
  • Determining the structure and function of the SUMO targeted ubiquitin E3 ligase RNF4.
  • Defining the pathway that leads to degradation of the Promyelocytic Leukaemia protein during arsenic therapy for Acute promyelocytic Leukaemia.
  • Investigating system wide changes to SUMO modification in response to stress using high throughput quantitative proteomics.

Figure 1. Structure of NEDD8 specific protease NEDP1 (blue space fill) in a transition state complex with NEDD8 (pink ribbon diagram). It shows the C-terminus of NEDD8 disappearing into the NEDP1 cleavage tunnel. From Shen LN, Liu H, Dong C, Xirodimas D, Naismith JH, Hay RT. (2005) Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1. EMBO J. 24: 1341-51.

Selected Publications

Plechanovova A, Jaffray EG, McMahon SA, Johnson KA, Navratilova I, Naismith JH, Hay RT. (2011) Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nature Structural and Molecular Biology 18:1052-9.

Tatham MH, Matic I, Mann M, Hay RT. (2011) Comparative Proteomic Analysis Identifies a Role for SUMO in Protein Quality Control. Science Signaling. 4: rs4.

Bruderer R, Tatham MH, Plechanovova A, Matic I, Garg AK, Hay RT. (2011) Purification and identification of endogenous polySUMO conjugates. EMBO Reports. 12:142-8.

Hattersley N, Shen L, Jaffray EG, Hay RT. (2011) The SUMO protease SENP6 is a direct regulator of PML nuclear bodies. Mol Biol Cell. 22: 78-90.

Geoffroy MC, Jaffray EG, Walker KJ, Hay RT. (2010) Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies. Mol Biol Cell. 21: 4227-39.

Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT. System-wide changes to SUMO modifications in response to heat shock. (2009) Science Signaling. 2: ra24

Shen LN, Geoffroy MC, Jaffray EG, Hay RT. (2009) Characterization of SENP7, a SUMO-2/3-specific isopeptidase. Biochem Journal 421: 223-30.

Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT. (2008) RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nature Cell Biology. 10: 538-546.

Xirodimas DP, Sundqvist A, Nakamura A, Shen L, Botting C, Hay RT. (2008) Ribosomal proteins are targets for the NEDD8 pathway. EMBO Reports. 9: 280-286.



Goethe University


Role of the SUMO specific ubiquitin ligase RNF4 in the DNA damage response.