Journal
NUCLEIC ACIDS RESEARCH
Volume 45, Issue 11, Pages 6259-6264Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkx446
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Funding
- Deutsche Forschungsgemeinschaft (Cluster of Excellence Cellular Stress Responses in Aging-Associated Diseases) [EXC 229]
- European Union [657501]
- Deutsche Forschungsgemeinschaft [EXC 229]
- Marie Curie Actions (MSCA) [657501] Funding Source: Marie Curie Actions (MSCA)
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Protein ADP-ribosylation (ADPr), a biologically and clinically important post-translational modification, exerts its functions by targeting a variety of different amino acids. Its repertoire recently expanded to include serine ADPr, which is emerging as an important and widespread signal in the DNA damage response. Chemically, serine ADPr (andmore generally o-glycosidic ADPr) is a form of o-glycosylation, and its extreme lability renders it practically invisible to standard mass spectrometry approaches, often leading to erroneous localizations. The knowledge from the mature field of o-glycosation and our own initial difficulties with mass spectrometric analyzes of serine ADPr suggest how to avoid these misidentifications and fully explore the scope of o-glycosidic ADPr in DNA damage response and beyond.
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