Laboratory of mono(ADP-ribosyl)ation

Post-translational modifications of proteins can influence for example their localisation, stability and interactions. They are important throughout life, from early development to being deregulated in disease. Some are well studied, like phosphorylation or ubiquitination, others remain more obscure still. We are interested in the modification of proteins with ADP-ribose.

Of long unknown importance, slowly its functions are emerging, such as in innate immunity and metabolism. We are interested in both the enzymes that add ADP-ribose to proteins, the PARPs or ARTDs, and the enzymes that remove it, the macrodomain-containing hydrolases. By determining these enzymes’ function in in vitro and in vivo systems, we intend to further uncover the processes influenced by mono(ADP-ribosyl)ation. This will then enable us to decipher where ADP-ribosylation goes wrong in disease onset and progression.

Pruneda*, J. N., R. Zaja*, M. S. Cohen* and K. L. H. Feijs-Zaja* (2025). "The emergence of MARUbylation as a hybrid ubiquitin and ADP-ribose modification." Nat Rev Mol Cell Biol. 26(11):820-1.

Ikenga NJ, J. Vervoorts, B. Luscher, R. Zaja*, K. L. H. Feijs-Zaja* (2025). PARP7 is a proteotoxic stress sensor that labels proteins for degradation. EMBO J. 44(19):5463-81.

Weixler, L., R. Zaja*, N. J. Ikenga, J. Siefert, G. Mohan, G. Aydin, S. Wijngaarden, D. V. Filippov, B. Luscher and K. L. H. Feijs-Zaja* (2025). "Family-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase." Commun Biol 8(1): 453.

Feijs-Zaja, K. L. H.*, N. J. Ikenga and R. Zaja (2024). "Pathological and physiological roles of ADP-ribosylation: established functions and new insights." Biol Chem 405(9-10): 567-581.

Weixler, L., N. J. Ikenga, J. Voorneveld, G. Aydin, T. M. Bolte, J. Momoh, M. Butepage, A. Golzmann, B. Luscher, D. V. Filippov, R. Zaja* and K. L. Feijs* (2023). "Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used." Life Sci Alliance 6(1).

Vogt, S., K. Feijs, S. Hosch, R. De Masi, R. Lintermann, B. Loll and L. Wirthmueller (2022). "The superior salinity tolerance of bread wheat cultivar Shanrong No. 3 is unlikely to be caused by elevated Ta-sro1 poly-(ADP-ribose) polymerase activity." Plant Cell 34(11): 4130-4137.

Feijs, K. L. H.* and R. Zaja (2022). "Are PARPs promiscuous?" Biosci Rep 42(5).

Weixler, L., K. L. H. Feijs* and R. Zaja* (2022). "ADP-ribosylation of RNA in mammalian cells is mediated by TRPT1 and multiple PARPs." Nucleic Acids Res 50(16): 9426-9441.

Luscher, B., I. Ahel, M. Altmeyer, A. Ashworth, P. Bai, P. Chang, M. Cohen, D. Corda, F. Dantzer, M. D. Daugherty, T. M. Dawson, V. L. Dawson, S. Deindl, A. R. Fehr, K. L. H. Feijs, D. V. Filippov, J. P. Gagne, G. Grimaldi, S. Guettler, N. C. Hoch, M. O. Hottiger, P. Korn, W. L. Kraus, A. Ladurner, L. Lehtio, A. K. L. Leung, C. J. Lord, A. Mangerich, I. Matic, J. Matthews, G. L. Moldovan, J. Moss, G. Natoli, M. L. Nielsen, M. Niepel, F. Nolte, J. Pascal, B. M. Paschal, K. Pawlowski, G. G. Poirier, S. Smith, G. Timinszky, Z. Q. Wang, J. Yelamos, X. Yu, R. Zaja and M. Ziegler (2022). "ADP-ribosyltransferases, an update on function and nomenclature." FEBS J 289(23): 7399-7410.

Weixler, L., K. Scharinger, J. Momoh, B. Luscher, K. L. H. Feijs* and R. Zaja* (2021). "ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function." Nucleic Acids Res 49(7): 3634-3650.