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.
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
Interplay of Histone Marks with Serine ADP-Ribosylation
Bartlett, E., Bonfiglio, J. J., Prokhorova, E., Colby, T., Zobel, F., Ahel, I., Matic, I.
(2018) Cell Rep, 24, 13, 3488-3502 e5
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
|2019||ERC Consolidator Grant - nbPTMs - European Research Council, 2021-2026|
|2018||EMBO Young Investigator programme (2019 - 2023)|
|2014||Marie Skłodowska-Curie fellowship (selected as an EU Success Story by the European Commission) to Dr. Bonfiglio|
|2009||Sir Henry Wellcome postdoctoral fellowship/grant - Wellcome Trust, UK, 2010-2014|