Related Experiment Video
Updated: Jul 13, 2026

Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog
Published on: November 5, 2014
PARPs and ADP-ribosylation-mediated biomolecular condensates: determinants, dynamics, and disease implications
Hongrui Liu1, Meenakshi Pillai2, Anthony K L Leung3
1Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA; Cross-Disciplinary Graduate Program in Biomedical Sciences (XDBio), School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA.
Abstract:
Biomolecular condensates are cellular compartments that selectively enrich proteins and other macromolecules despite lacking enveloping membranes. These compartments often form through phase separation triggered by multivalent nucleic acids. Emerging data have revealed that poly(ADP-ribose) (PAR), a nucleic acid-based protein modification catalyzed by ADP-ribosyltransferases (commonly known as PARPs), plays a crucial role in this process. This review focuses on the role of PARPs and ADP-ribosylation, and explores the principles and mechanisms by which PAR regulates condensate formation, dissolution, and dynamics. Future studies with advanced tools to examine PAR binding sites, substrate interactions, PAR length and structure, and transitions from condensates to aggregates will be key to unraveling the complexity of ADP-ribosylation in health and disease, including cancer, viral infection, and neurodegeneration.
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Riboswitches
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
Directing Proteins to the Rough Endoplasmic Reticulum
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Regulation of the Unfolded Protein Response
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.

