University of Dundee

Centre for Gene Regulation and Expression

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New class of E3 ligase discovered by Virdee lab in collaboration with van Aalten lab

Dr Virdee and colleagues in the Medical Research Council Protein Phosphorylation and Ubiquitylation Unit (MRC PPU) have discovered a novel class of E3 ligase. The E3 ligase, MYCBP2, operates in a unique way, selectively transferring ubiquitin to non-lysine amino acids with selectivity for threonine. The ubiquitin is linked to the threonine amino acid via a chemically distinct ester linkage thereby uncovering an unanticipated area of cellular biology. The findings are published in Nature.

The Image Data Resource is added to the list of Scientific Data recommended data repositories

Nature Research journal Scientific Data is a peer-reviewed, open-access journal for descriptions of scientifically valuable datasets, and research that advances the sharing and reuse of scientific data. These data descriptors provide a path for publishing datasets associated with scientific publications.

Dundee scientists solve 3D structure of key protein involved in Intellectual Disability

Scientists in the School have identified the effects of a mutation that gives rise to a form of Intellectual Disability.

Intellectual Disability is a type of developmental brain disorder in young patients which to date remains poorly understood and is incurable. Researchers focussed on mutations in the OGT gene, which plays a critical role in protecting brain cells against stress. In patients harbouring OGT mutations, this protective effect is lost.


The Pelisch Lab seeks a Research Technician to work as part of a team exploring the role of SUMOylation and other post-translational modifications during cell division. We use a combination of genetics, biochemistry and live microscopy.

Pelisch et al, A SUMO-dependent protein network regulates chromosome congression during oocyte meiosis. Molecular Cell (2017), 65:66-77.

Pelisch, F.* & Hay, R.T. Tools to study SUMO conjugation in C. elegans. Methods Mol Biol. 2016;1475:233-56. doi: 10.1007/978-1-4939-6358-4_17.