Niels Mailand

Niels Mailand

Professor, head of research

Work in my laboratory aims to understand how signaling processes, in particular those mediated by ubiquitin and ubiquitin-like modifier proteins, orchestrate and regulate cellular responses to DNA damage and replication stress to safeguard genome stability in human cells. The correct functioning of these processes is of fundamental importance for avoiding a multitude of severe pathologies including cancer and neurodegenerative disorders that can arise as a consequence of genetic changes. While it is clear that protective cellular responses to genotoxic insults are driven by coordinated post-translational modifications of the numerous proteins involved, a comprehensive understanding of the scope, dynamics and functions of these crucial yet highly complex processes is lacking.
We are addressing this challenge by combining targeted cell biology-, biochemistry- and microscopy-driven approaches with cutting-edge systems-wide screening strategies to illuminate the signaling responses promoting genome stability maintenance on both a global and mechanistic level.
Our work has led to the identification of an extensive range of new proteins involved in genome stability maintenance, and elucidated in mechanistic detail how signaling via ubiquitin and related modifier proteins underpins the DNA damage response.

Current studies in my lab focus on applying innovative approaches for illuminating cellular roles and mechanisms of understudied genome surveillance factors, ubiquitin chain types and DNA repair pathways, and exploring new and unexpected crosstalk between the DNA damage response and other cellular machineries.

Selected publications

  1. Published

    ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability

    Haahr, Peter Thorlund, Borgermann, N., Guo, X., Typas, D., Achuthankutty, D., Hoffmann, Saskia, Shearer, Robert Francis, Sixma, T. K. & Mailand, Niels, 2018, In: Molecular Cell. 70, 1, p. 165-174

    Research output: Contribution to journalJournal articlepeer-review

  2. Published

    Activation of the ATR kinase by the RPA-binding protein ETAA1

    Haahr, Peter Thorlund, Hoffmann, Saskia, Tollenaere, M. A. X., Ho, T., Toledo Lazaro, L. I., Mann, Matthias, Bekker-Jensen, Simon Holst, Räschle, M. & Mailand, Niels, Nov 2016, In: Nature Cell Biology. 18, 11, p. 1196–1207

    Research output: Contribution to journalJournal articlepeer-review

  3. Published

    Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage

    Thorslund, T., Ripplinger, A., Hoffmann, Saskia, Wild, T., Uckelmann, M., Villumsen, B., Narita, Takeo, Sixma, T. K., Choudhary, Chunaram, Bekker-Jensen, Simon Holst & Mailand, Niels, 19 Nov 2015, In: Nature. 527, 7578, p. 389-93 5 p.

    Research output: Contribution to journalLetterpeer-review

  4. Published

    Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links

    Räschle, M., Smeenk, G., Hansen, R. K., Temu, T., Oka, Y., Hein, M. Y., Nagaraj, N., Long, D. T., Walter, J. C., Hofmann, K., Storchova, Z., Cox, J., Bekker-Jensen, Simon Holst, Mailand, Niels & Mann, Matthias, 2015, In: Science. 348, 6234, p. 539- 10 p., 1253671.

    Research output: Contribution to journalJournal articlepeer-review

  5. Published

    Ubiquitin-SUMO Circuitry Controls Activated Fanconi Anemia ID Complex Dosage in Response to DNA Damage

    Gibbs-Seymour, I., Oka, Y., Rajendra, E., Weinert, B. T., Passmore, L. A., Patel, K. J., Olsen, Jesper Velgaard, Choudhary, Chunaram, Bekker-Jensen, Simon Holst & Mailand, Niels, Jan 2015, In: Molecular Cell. 57, 1, p. 150-64 15 p.

    Research output: Contribution to journalJournal articlepeer-review

  6. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins

    Mailand, Niels, Bekker-Jensen, Simon Holst, Faustrup, H., Melander, F., Bartek, J., Lukas, Claudia & Lukas, Jiri, 2007, In: Cell. 131, 5, p. 887-900 14 p.

    Research output: Contribution to journalJournal articlepeer-review

ID: 13844358