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Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
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Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
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Journal Article
Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
2013
Overview
A proteomic method to identify human proteins post-translationally modified by poly(ADP-ribosyl)ation is reported, which will help yield further insights into the biological role of this modification.
Poly(ADP-ribosyl)ation is catalyzed by a family of enzymes known as PARPs. We describe a method to characterize the human aspartic acid– and glutamic acid–ADP-ribosylated proteome. We identified 1,048 ADP-ribosylation sites on 340 proteins involved in a wide array of nuclear functions; among these were many previously unknown PARP downstream targets whose ADP-ribosylation was sensitive to PARP inhibitor treatment. We also confirmed that iniparib had a negligible effect on PARP activity in intact cells.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Adenosine Diphosphate Ribose - chemistry
/ Adenosine Diphosphate Ribose - genetics
/ Adenosine Diphosphate Ribose - metabolism
/ Biomedical Engineering/Biotechnology
/ Enzymes
/ Glycoside Hydrolases - chemistry
/ Glycoside Hydrolases - genetics
/ Glycoside Hydrolases - metabolism
/ Humans
/ Hydrogen Peroxide - pharmacology
/ Mutation
/ Poly (ADP-Ribose) Polymerase-1
/ Poly(ADP-ribose) Polymerase Inhibitors
/ Poly(ADP-ribose) Polymerases - chemistry
/ Poly(ADP-ribose) Polymerases - genetics
/ Poly(ADP-ribose) Polymerases - metabolism
/ Post-translational modification
/ Protein Processing, Post-Translational
/ Proteins
/ Sugars
