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EMBO Member

Ronald T. Hay

University, Dundee | United Kingdom

EMBO 2009

The biology of SUMO and ubiquitin conjugation

My laboratory established conjugation with the Small Ubiquitin-like Modifier (SUMO) as an important regulatory mechanism in eukaryotes. We demonstrated that poly-SUMO chains could act as recognition sites for the ubiquitin ligase Rnf4. This targets Promyelocytic Leukaemia (PML) protein for arsenic-induced, ubiquitin-mediated proteolysis and establishes the molecular basis of arsenic therapy in the treatment of leukaemia.

Keywords: SUMO / ubiquitin / E3 ligase / SUMO protease / RNF4

Subject area(s): Genome Stability & Dynamics | Proteins & Biochemistry | Structural Biology & Biophysics