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Serine ADP-ribosylation depends on HPF1

ABSTRACT: We report that serine ADPr is strictly dependent on HPF1 (histone PARylation factor 1. Quantitative proteomics revealed that serine ADPr does not occur in cells lacking HPF1. We identified three endogenous serine ADPr sites are located on the PARP-1 automodification domain. Further identification of serine ADPr on hundreds of other targets indicates that serine ADPr is a widespread modification.

INSTRUMENT(S): Orbitrap Fusion ETD, Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Juan Jose Bonfiglio

LAB HEAD: Ivan Matic

PROVIDER: PXD005627 | Pride | 2017-02-10

REPOSITORIES: Pride

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Serine ADP-Ribosylation Depends on HPF1.

Bonfiglio Juan José JJ Fontana Pietro P Zhang Qi Q Colby Thomas T Gibbs-Seymour Ian I Atanassov Ilian I Bartlett Edward E Zaja Roko R Ahel Ivan I Matic Ivan I

Molecular cell 20170209 5

ADP-ribosylation (ADPr) regulates important patho-physiological processes through its attachment to different amino acids in proteins. Recently, by precision mapping on all possible amino acid residues, we identified histone serine ADPr marks in the DNA damage response. However, the biochemical basis underlying this serine modification remained unknown. Here we report that serine ADPr is strictly dependent on histone PARylation factor 1 (HPF1), a recently identified regulator of PARP-1. Quantita ...[more]

PMID: 28190768

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