Dr. Daniel Salas Lloret


I am trained as a biochemist with master in biotechnology and I have worked in different fields but with a common final aim, fighting cancer. During my PhD, we developed a Mass-Spectrometry tool termed TULIP2 which allows the identification of specific targets for an ubiquitin E3 ligase of interest. Additionally, we modified this technology to find specific targets for SUMO E3 ligases which we named SATT. We employed different SATTs to provide the first comprehensive E3-specific sumo proteome. My PhD was funded by the KWF to find targets for the ubiquitin E3 ligase BRCA1/BARD1. To fulfill this task, we employed the TULIP2 methodology and we found PCNA as the main ubiquitination target for BRCA1/BAD1 in unperturbed conditions. We demonstrated that BRCA1/BARD1 ubiquitinates PCNA to solved ssDNA gaps during replication to maintain genomic stability. Cancer cells lacking BRCA1/BARD1 E3 ligase activity present replication problems. Employing compounds such as hydroxyurea can disrupt the natural replication process and expose cancer cells. For my postdoc project, we use the SUMO inhibitor TAK981, which is in clinical trials, to understand how we can boost the immune system to tackle cancer.



  • TULIP2: An Improved Method for the Identification of Ubiquitin E3-Specific Targets.

    Salas-Lloret, D., Agabitini, G., and Gonzalez-Prieto, R.

    Front Chem 2019, 7, 802.

  • Insights in Post-Translational Modifications: Ubiquitin and SUMO.

    D. Salas-Lloret, R. Gonzalez-Prieto

    Int J Mol Sci 23 (2022)

  • SUMO-activated target traps (SATTs) enable the identification of a comprehensive E3-specific SUMO proteome.

    D. Salas-Lloret et al.

    Sci Adv 9, eadh2073 (2023).


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