Ron Hay Background
Research
Publications
Current Lab

Professor Ron Hay
E: r.t.hay@dundee.ac.uk
T: 44 1382 386309
F: 44 1382 223778

Professor Ron Hay FRS FRSE - Honorary Programme Leader

Publications

2011
 

Larance, M., Bailly, A.P., Pourkarimi, E., Hay, R.T., Buchanan, G., Coulthurst, S., Xirodimas, D.P., Gartner, A., and Lamond, A.I. (2011). Stable-isotope labeling with amino acids in nematodes. Nat Methods 8, 849-851.

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Matic, I., Jaffray, E.G., Oxenham, S.K., Groves, M.J., Barratt, C.L., Tauro, S., Stanley-Wall, N.R., and Hay, R.T. (2011). Absolute SILAC-Compatible Expression Strain Allows Sumo-2 Copy Number Determination in Clinical Samples. J Proteome Res 10, 4869-4875.

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Plechanovova, A., Jaffray, E.G., McMahon, S.A., Johnson, K.A., Navratilova, I., Naismith, J.H., and Hay, R.T. (2011). Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nat Struct Mol Biol 18, 1052-1059.

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Tatham, M.H., Matic, I., Mann, M., and Hay, R.T. (2011). Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal 4, rs4.

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Bruderer, R., Tatham, M.H., Plechanovova, A., Matic, I., Garg, A.K., and Hay, R.T. (2011). Purification and identification of endogenous polySUMO conjugates. EMBO Rep 12, 142-148.

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Hattersley, N., Shen, L., Jaffray, E.G., and Hay, R.T. (2011). The SUMO protease SENP6 is a direct regulator of PML nuclear bodies. Mol Biol Cell 22, 78-90.

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Napolitano, L.M., Jaffray, E.G., Hay, R.T., and Meroni, G. (2011). Functional interactions between ubiquitin E2 enzymes and TRIM proteins. Biochem J 434, 309-319.

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2010
 

Li, X., Vadrevu, S., Dunlop, A., Day, J., Advant, N., Troeger, J., Klussmann, E., Jaffrey, E., Hay, R.T., Adams, D.R., Houslay, M.D. and Baillie, G.S. (2010). Selective SUMO modification of cAMP-specific phosphodiesterase-4D5 (PDE4D5) regulates the functional consequences of phosphorylation by PKA and ERK. Biochem J 428, 55-65.

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Hjerpe, R., Aillet, F., Lopitz-Otsoa, F., Lang, V., Torres-Ramos, M., Farras, R., Hay, R.T., and Rodriguez, M.S. (2010). Oligomerization conditions Mdm2-mediated efficient p53 polyubiquitylation but not its proteasomal degradation. Int J Biochem Cell Biol 42, 725-735.

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Golebiowski, F., Tatham, M.H., Nakamura, A., and Hay, R.T. (2010). High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties. Nat Protoc 5, 873-882.

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Hannoun, Z., Greenhough, S., Jaffray, E., Hay, R.T., and Hay, D.C. (2010). Post-translational modification by SUMO. Toxicology 278, 288-293.

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Castillo-Lluva, S., Tatham, M.H., Jones, R.C., Jaffray, E.G., Edmondson, R.D., Hay, R.T., and Malliri, A. (2010). SUMOylation of the GTPase Rac1 is required for optimal cell migration. Nat Cell Biol 12, 1078-1085.

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Geoffroy, M.C., Jaffray, E.G., Walker, K.J., and Hay, R.T. (2010). Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies. Mol Biol Cell 21, 4227-4239.

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2009
 

Geoffroy, M.C., and Hay, R.T. (2009). An additional role for SUMO in ubiquitin-mediated proteolysis. Nat Rev Mol Cell Biol 10, 564-568.

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Golebiowski, F., Matic, I., Tatham, M.H., Cole, C., Yin, Y., Nakamura, A., Cox, J., Barton, G.J., Mann, M., and Hay, R.T. (2009). System-wide changes to SUMO modifications in response to heat shock. Sci Signal 2, ra24.

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Shen, L.N., Geoffroy, M.C., Jaffray, E.G., and Hay, R.T. (2009). Characterization of SENP7, a SUMO-2/3-specific isopeptidase. Biochem J 421, 223-230.

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Tatham, M.H., and Hay, R.T. (2009). FRET-based in vitro assays for the analysis of SUMO protease activities. Methods Mol Biol 497, 253-268.

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2008
 

Miles, W.O., Jaffray, E., Campbell, S.G., Takeda, S., Bayston, L.J., Basu, S.P., Li, M., Raftery, L.A., Ashe, M.P., Hay, R.T., and Ashe, H.L. (2008). Medea SUMOylation restricts the signaling range of the Dpp morphogen in the Drosophila embryo. Genes Dev 22, 2578-2590.

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Tatham, M.H., Geoffroy, M.C., Shen, L., Plechanovova, A., Hattersley, N., Jaffray, E.G., Palvimo, J.J., and Hay, R.T. (2008). RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol 10, 538-546.

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Agostinho, M., Santos, V., Ferreira, F., Costa, R., Cardoso, J., Pinheiro, I., Rino, J., Jaffray, E., Hay, R.T., and Ferreira, J. (2008). Conjugation of human topoisomerase 2 alpha with small ubiquitin-like modifiers 2/3 in response to topoisomerase inhibitors: cell cycle stage and chromosome domain specificity. Cancer Res 68, 2409-2418.

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Martin, S.F., Tatham, M.H., Hay, R.T., and Samuel, I.D. (2008). Quantitative analysis of multi-protein interactions using FRET: application to the SUMO pathway. Protein Sci 17, 777-784.

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Xirodimas, D.P., Sundqvist, A., Nakamura, A., Shen, L., Botting, C., and Hay, R.T. (2008). Ribosomal proteins are targets for the NEDD8 pathway. EMBO Rep 9, 280-286.

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Matic, I., van Hagen, M., Schimmel, J., Macek, B., Ogg, S.C., Tatham, M.H., Hay, R.T., Lamond, A.I., Mann, M., and Vertegaal, A.C. (2008). In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol Cell Proteomics 7, 132-144.

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2007
 

Hay, R.T. (2007). SUMO-specific proteases: a twist in the tail. Trends Cell Biol 17, 370-376.

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Tillmanns, S., Otto, C., Jaffray, E., Du Roure, C., Bakri, Y., Vanhille, L., Sarrazin, S., Hay, R.T., and Sieweke, M.H. (2007). SUMO modification regulates MafB-driven macrophage differentiation by enabling Myb-dependent transcriptional repression. Mol Cell Biol 27, 5554-5564.

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Jacobs, A.M., Nicol, S.M., Hislop, R.G., Jaffray, E.G., Hay, R.T., and Fuller-Pace, F.V. (2007). SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1. Oncogene 26, 5866-5876.

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Meinecke, I., Cinski, A., Baier, A., Peters, M.A., Dankbar, B., Wille, A., Drynda, A., Mendoza, H., Gay, R.E., Hay, R.T., Ink, B., Gay, S. and Pap, T. (2007). Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts. Proc Natl Acad Sci U S A 104, 5073-5078.

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Dorval, V., Mazzella, M.J., Mathews, P.M., Hay, R.T., and Fraser, P.E. (2007). Modulation of Abeta generation by small ubiquitin-like modifiers does not require conjugation to target proteins. Biochem J 404, 309-316.

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Martin, S.F., Hattersley, N., Samuel, I.D., Hay, R.T., and Tatham, M.H. (2007). A fluorescence-resonance-energy-transfer-based protease activity assay and its use to monitor paralog-specific small ubiquitin-like modifier processing. Anal Biochem 363, 83-90.

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Janssen, K., Hofmann, T.G., Jans, D.A., Hay, R.T., Schulze-Osthoff, K., and Fischer, U. (2007). Apoptin is modified by SUMO conjugation and targeted to promyelocytic leukemia protein nuclear bodies. Oncogene 26, 1557-1566.

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