María completed her Master's in Molecular Biology and Biomedicine at the University of the Basque Country. During her time at Rosa Barrio´s Lab (CICbioGUNE, Bilbao, Spain), she worked on the characterisation of the Townes Brocks Syndrome, a rare genetic disease and surprisingly a recently described ciliopathy. With a strong interest in genetics, she soon became very attracted to the proteomic field, and more specifically to the ubiquitin code. As part of her PhD thesis, María set up conditions for mass spectrometry analysis of bortezomib resistant cells using biotinylated TUBEs and chain specific nanobodies. Furthermore she inhibited ubiquitin enzymes using various approaches to analyse the impact of these enzymes in the composition of ubiquitin chains and resistance to bortezomib.

Grégoire joined the lab after a Master's degree at the INSA engineering school. During his Phd, Grégoire studied the role of ubiquitin like proteins in the UPS-ALS crosstalk in Bortezomib resistant Mantle Cell lymphoma (MCL).  He has demonstrated that autophagy is upregulated in MCL cells that resist to proteasome inhibitors. In particular, proteaphagy plays a crucial role when the proteasome is impaired. The autophagy receptor p62 plays a crucial role in the autophagosome formation and its inhibiton blocks proteaphagy en favors apoptosis of bortezomib resistant cells. Grégoire also developed LC3-traps to capture and analyse autophagosome formation and regulation.

Rosa's PhD project aimed at analysing the proteasome-autophagy crosstalk under proteotoxic stress conditions in Acute Myeloid Leukaemia (AML).  This thesis was oriented to understand the UPS-ALS crosstalk under proteasome inhibition conditions. Rosa Lopez Reyes was interested in characterising selective autophagy envents activated after bortezomib treatment and in particular, proteaphagy.

Lydia's PhD thesis focused on the identification of new therapeutic targets and inhibitors of the ubiquitin-proteasome system (UPS) for malaria treatment. The two major objectives of this research were to identify ub-regulated processes/targets controlling the erythrocytic cycle of Plasmodium falciparum that could represent targets for intervention, and to identify new inhibitors of the UPS that will selectively target Plasmodium falciparum. The two objectives were successfully achieved and these results are currently exploited by GlaxoSmithKline (GSK).

Lydia Mata-Cantero now holds a permanent position at GSK-Madrid.

As part of her PhD, Sofia used mass spectrometry-based proteomics strategies to define protein NEDDylation. The major goal of this work was the implementation of a methodology to identify NEDD8 signatures by mass spectrometry. The obtained results underlined a crucial role of NEDD8 in the regulation of proteotoxic stress.

Sofia Lobato-Gil is now a post-doctoral fellow at the IMB (Institute of Molecular Biology), Mainz, Germany (supervisor Dr. Petra Beli).

During her PhD, Elisa contributed to the development and optimisation of the SUMO-traps (SUBEs) and their application to isolate and study SUMOylated proteins in the regulation of essential cancer cellular factors. She then went on a postdoc at the Faculty of Medicine of the University of Coimbra, where she studied the molecular interactions between ubiquitin-like proteins and autophagy in regulation of the gap-juction protein Conexin 43 using ischemia-reperfusion models.

During his PhD, Roland worked on developing the Tandem Ubiquitin Binding Entities (TUBEs) and applied them to p53 regulation. He then went on for a postdoc in at the MRC-PPU in Scotland, before joining Sygnature in 2017.

Roland is now working as a team leader at Sygnature Discovery, a contract research organization (CRO) specializing in pre-clinical drug discovery.