ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification

Qiang Liu; Bogdan I Florea; Dmitri V Filippov

doi:10.1016/j.chembiol.2017.04.003

ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification

Cell Chem Biol. 2017 Apr 20;24(4):431-432. doi: 10.1016/j.chembiol.2017.04.003.

Authors

Qiang Liu¹, Bogdan I Florea¹, Dmitri V Filippov²

Affiliations

¹ Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, the Netherlands.
² Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, the Netherlands. Electronic address: filippov@chem.leidenuniv.nl.

PMID: 28431224
DOI: 10.1016/j.chembiol.2017.04.003

Abstract

Proteins containing adenosine diphosphate ribosylserine as a posttranslational modification are widespread and formed via HPF1-assisted, PARP-1-mediated PARylation as Bonfiglio et al. (2017) report in a recent issue of Molecular Cell.

Publication types

Comment

MeSH terms

ADP-Ribosylation
Poly(ADP-ribose) Polymerases / genetics*
Protein Processing, Post-Translational
Serine*

Substances

Serine
Poly(ADP-ribose) Polymerases