Thomas Williams, a PDRA in the Rousseau group of the MRC PPU has been awarded the Brian Cox for excellence in public engagement engaged researcher award. This award is awarded to a researcher who has made an outstanding contribution in communicating science performed within the University of Dundee School of Life Sciences.

Thomas Williams from the Rousseau group of the MRC PPU have been awarded the University of Dundee Molecular and Cellular Biology prize for unravelling a mechanism underpinning increased translation of proteasome assembly chaperones followed stress.

Ana Cuenda, who carried out postdoctoral research in the Medical Research Council Protein Phosphorylation Unit at the University of Dundee from 1994 to 1999 has had a street in Spain named after her (named Calle Ana Cuenda).

Phosphorylation is a reversible post-translational modification bestowed on proteins, by which phosphate is added or removed from protein substrates. Reversible phosphorylation is capable of regulating proteins in virtually every conceivable way.

Researchers have uncovered multiple phosphorylation sites in the protein Shp1/p47 that are altered in response to cell stress. This finding could be important for understanding the regulation of cellular quality control pathways linked to diseases such as cancer and neurodegeneration.

Dario Alessi has been named as the winner of the 2023 Jeantet-Collen Prize for Translational Medicine. The award is given by the Louis-Jeantet Foundation.

It is with great sadness that we report the death of Mark Peggie, Head of the MRC PPU’s cloning team for many years, who died suddenly on January 17th 2023 at the age of 54.

Tom Williams, who has been working as a postdoctoral researcher in Adrien Rousseau’s group since 2019 has been awarded the British Society for Cell Biology (BSCB) postdoctoral researcher medal for 2023.

We are delighted to announce that our latest MRC PPU group leader, Chiara Maniaci, has now opened her laboratory.

For many years, it has thought that eight types of ubiquitin chain can be formed in cells in which the C-terminal carboxylate of ubiquitin forms isopeptide bonds with the ε-amino group of any of the seven lysine residues in another ubiquitin molecule or a peptide bond with the α-amino group of the N-terminal methionine residue of another ubiquitin (Met1-linked ubiquitin).