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Serine ADP-ribosylation reversal by the hydrolase ARH3

MPG-Autoren

Fontana,  P.*
Max Planck Institute for Biology of Ageing, Max Planck Society;

Bonfiglio,  J. J.*
Max Planck Institute for Biology of Ageing, Max Planck Society;

Palazzo,  L.*
Max Planck Institute for Biology of Ageing, Max Planck Society;

Bartlett,  E.
Max Planck Institute for Biology of Ageing, Max Planck Society;

Matic,  I.**
Max Planck Institute for Biology of Ageing, Max Planck Society;

Ahel,  I.**
Max Planck Institute for Biology of Ageing, Max Planck Society;

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Zitation

Fontana, P., Bonfiglio, J. J., Palazzo, L., Bartlett, E., Matic, I., & Ahel, I. (2017). Serine ADP-ribosylation reversal by the hydrolase ARH3. Elife, 6. doi:10.7554/eLife.28533.


Zitierlink: http://hdl.handle.net/21.11116/0000-0001-5903-8
Zusammenfassung
ADP-ribosylation (ADPr) is a posttranslational modification (PTM) of proteins that controls many cellular processes, including DNA repair, transcription, chromatin regulation and mitosis. A number of proteins catalyse the transfer and hydrolysis of ADPr, and also specify how and when the modification is conjugated to the targets. We recently discovered a new form of ADPr that is attached to serine residues in target proteins (Ser-ADPr) and showed that this PTM is specifically made by PARP1/HPF1 and PARP2/HPF1 complexes. In this work, we found by quantitative proteomics that histone Ser-ADPr is reversible in cells during response to DNA damage. By screening for the hydrolase that is responsible for the reversal of Ser-ADPr, we identified ARH3/ADPRHL2 as capable of efficiently and specifically removing Ser-ADPr of histones and other proteins. We further showed that Ser-ADPr is a major PTM in cells after DNA damage and that this signalling is dependent on ARH3.