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Accueil > Animation scientifique & Evénements > Conférences CICB-Paris > Archives des conférences CICB-Paris de 2015

SUMO as a signal for ubiquitin modification

SUMO, un signal pour la modification par l’Ubiquitine

par Marie Körner - publié le , mis à jour le

par Prof. Ronald Hay

Cette conférence se tiendra le jeudi 26 mars, de 11-13h dans la salle de conférence R229


Ron Hay is Professor of Molecular Biology at the Centre for Gene Regulation and Expression and Honorary member of theMRC Protein Phosphorylation and Ubiquitination Unit, University of Dundee. He attended Heriot-Watt University, Edinburgh and obtained his PhD from the University of Glasgow. His postdoctoral research was carried out at Harvard Medical School, Boston before joining the MRC Virology Unit, Glasgow as an Independent Investigator. In 1985 he Joined the Biochemistry Department of the University of St Andrews and in 2005 took up his present position in Dundee. Ron’s work focuses on establishing the roles of Ubiquitin and Small Ubiquitin-like Modifier (SUMO) as signaling components. Ron is a Wellcome Trust Senior Investigator and a fellow of the Royal Society, the Royal Society of Edinburgh, the Academy of Medical Sciences, Academia Europaea and is a member of the European Molecular Biology Organisation. In 2012 Ron was awarded the Novartis Medal and Prize of the Biochemical Society.

Summary of talk

Small Ubiquitin-like Modifier (SUMO) appears to have over a thousand substrates and plays diverse roles in many important biological processes. Recognition of SUMO is mediated by short sequences of amino acids known as SUMO interaction motifs (SIMs) that allow effector proteins to engage SUMO modified substrates. Similarly to ubiquitin SUMO can form isopeptide linked chains and these polymers can be recognized by proteins containing multiple SIMs. One protein that contains such a sequence of SIMs also contains a dimeric RING domain that is the hallmark of a ubiquitin E3 ligase. This protein, known as RNF4, has the ability to recognize SUMO modified proteins and target them for ubiquitin modification and is a member of the family of SUMO Targeted Ubiquitin Ligases (STUbL). Dimeric RING E3 ligases interact with protein substrates and with an E2 conjugating enzyme that is thioester linked to ubiquitin. The RINGs function by binding both the E2 and ubiquitin in a conformation that is primed for catalysis. RNF4 can work with different E2 enzymes to generate different ubiquitin chain types. Interaction with Ubc5 leads to the formation of K48 linked ubiquitin while interaction with Ube2W leads to N-terminal monoubiquitination and interaction with Ubc13/Uev2 leads to the formation of K63 linked ubiquitin. I will discuss the mechanisms that lead to RNF4 activation and E2 mediated ubiquitin transfer.


Tammsalu T, Matic I, Jaffray EG, Ibrahim AFM, Tatham MH and Hay RT (2014) Proteome-wide Identification of SUMO2 Modification Sites. Science Signaling 7 : rs2.

Rojas-Fernandez A, Plechanovová A, Hattersley N, Jaffray EG, Tatham MH and Hay RT (2014) SUMO chain induced dimerisation activates RNF4. Molecular Cell 53 : 880-892.

Plechanovová A, Jaffray E, Tatham MH, Naismith JH, Hay RT. (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489, 115-120

Yin Y, Seifert A, Chua JS, Maure J-F, Golebiowski F, Hay RT. (2012) SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage. Genes and Development 26:1196-1208

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