Research Group Matić

ADP-ribosylation in DNA damage response and ageing

The proteins of a cell can be modified after their production. These dynamic and reversible modifications alter the function of proteins and are key contributors to cellular ageing and age-related diseases. Our research focuses on one type of protein modification, known as ADP-ribosylation. ADP-ribosylation is a versatile protein modification that plays critical roles in many physiological and pathological processes, from the DNA damage response and cancer to neurological disorders and aging. We are investigating the molecular mechanisms and biochemical processes involved in this protein modification and its role in DNA repair.

Many of the next significant advances in ageing research, from basic biology to clinical applications, will come from understanding the exact molecular mechanisms that underlie biological pathways whose relevance to ageing has been identified over the last decades. Determining the biochemical basis of a specific biological process often presents special challenges and requires new tools and approaches.

Our ambition is to reveal the elusive molecular mechanisms behind some of these ageing-relevant signaling pathways by applying our unique expertise in advanced proteomics and innovative chemical biology. The current aim of the Matic lab is to understand the molecular mechanisms of DNA damage response and ageing by elucidating the role of ADP-ribosylation in these biological processes.

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Selected Publications

Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Longarini, E. J., Matic, I.
(2024) Nat Commun, May 18, 2024

Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling
Longarini, E. J., Dauben, H., Locatelli, C., Wondisford, A. R., Smith, R., Muench, C., Kolvenbach, A., Lynskey, M. L., Pope, A., Bonfiglio, J. J., Jurado, E. P., Fajka-Boja, R., Colby, T., Schuller, M., 
Ahel, I., Timinszky, G., O’Sullivan, R. J., Huet, S., Matic, I.
(2023) Molecular Cell, published online: April 27, 2023; DOI

An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Bonfiglio, J. J., Leidecker, O., Dauben, H., Longarini, E. J., Colby, T., San Segundo-Acosta, P., Perez, K. A., Matic, I.
(2020) Cell, 183, 4, 1086-1102 e23

Serine ADP-Ribosylation Depends on HPF1
Bonfiglio, J. J., Fontana, P., Zhang, Q., Colby, T., Gibbs-Seymour, I., Atanassov, I., Bartlett, E., Zaja, R., Ahel, I., Matic, I.
(2017) Mol Cell, 65, 5, 932-940 e6

Serine is a new target residue for endogenous ADP-ribosylation on histones
Leidecker, O., Bonfiglio, J. J., Colby, T., Zhang, Q., Atanassov, I., Zaja, R., Palazzo, L., Stockum, A., Ahel, I., Matic, I.
(2016) Nat Chem Biol, 12, 12, 998-1000