As part of an active scientific community that studies the DNA damage response (DDR) and its impact on cancer and aging, research in the lab of Matthias Altmeyer is aimed at elucidating cellular mechanisms of genome integrity maintenance and their deregulation in human disease. Here you can explore who we are and what we do. Welcome!
A warm welcome to Virginia and Yannick
The lab warmly welcomes Virginia Pasti and Yannick Kok as new team members. Virginia will perform her Master thesis project with us, and Yannick joins as a new postdoc. Wishing both a successful start and exciting discoveries!
In a recent publication we identified replication stress-induced ssDNA lesions in G1 cells. They are found at telomeres in ALT-positive cancer cells and show signs of post-mitotic DNA synthesis (post-MiDAS).
Motivated applications from postdoc candidates with a strong interest in genome stability and willing to apply for fellowships are always encouraged. PhD students are recruited through the Life Science Zurich Graduate School.
Aleksandra’s paper is out in Nature Communications
RPA shields inherited DNA lesions for post-mitotic DNA synthesis
Fragile genomic regions undergo mitotic DNA synthesis (MiDAS). Aleksandra found evidence for post-mitotic DNA synthesis (post-MiDAS). Post-MiDAS occurs at telomeres, particularly in ALT-positive cancer cells, and is amplified by replication stress. Published in Nature Communications.
CHD7 and 53BP1 regulate distinct pathways for the re-ligation of DNA double-strand breaks
From a close collaboration with the lab of Haico van Attikum, and with great help from the labs of Sébastien Huet, Alfred Vertegaal, Jessica Downs and Martijn Luijsterburg, the chromatin remodeler CHD7 emerged as an early responder to DNA damage to regulate chromatin dynamics around DNA break sites and initiate repair. Finally out in Nature Communications.
Marco’s paper on TRIP12-regulated PARP inhibitor efficiency is out
The ubiquitin ligase TRIP12 limits PARP1 trapping and constrains PARP inhibitor efficiency
We found that the ubiquitin E3 ligase TRIP12, through its PAR-binding WWE domain, targets PARP1 for proteasomal degradation, affecting PARP functions and PARP inhibitor efficiency. Congratulations to Marco and big thanks to our collaborators Qingyao Huang and Michael Baudis for their help. Published in Cell Reports.