SERious Surprises for ADP-Ribosylation Specificity: HPF1 Switches PARP1 Specificity to Ser Residues

Anthony K L Leung

doi:10.1016/j.molcel.2017.02.012

SERious Surprises for ADP-Ribosylation Specificity: HPF1 Switches PARP1 Specificity to Ser Residues

Mol Cell. 2017 Mar 2;65(5):777-778. doi: 10.1016/j.molcel.2017.02.012.

Author

Anthony K L Leung¹

Affiliation

¹ Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA; Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA. Electronic address: anthony.leung@jhu.edu.

PMID: 28257697
DOI: 10.1016/j.molcel.2017.02.012

Abstract

In this issue of Molecular Cell, Bonfiglio et al. (2017) demonstrate that histone PARylation factor 1 (HPF1) is required for PARP1 to attach ADP-ribose groups onto the hydroxyl oxygen of the Ser residues of target substrates, including both PARP1 itself and histones. Here, mechanisms and implications of this unexpected, O-linked ADP-ribosylation are speculated on.

MeSH terms

Adenosine Diphosphate Ribose
Histones / chemistry*
Poly (ADP-Ribose) Polymerase-1
Poly(ADP-ribose) Polymerases / chemistry*

Substances

Histones
Adenosine Diphosphate Ribose
Poly (ADP-Ribose) Polymerase-1
Poly(ADP-ribose) Polymerases

Grants and funding

R01 GM104135/GM/NIGMS NIH HHS/United States