PARP Proteins, Signal Transduction Mechanisms and Chromatin Remodeling

Dear Colleagues,

Activated PARP proteins catalyze the post-translational modification of proteins by adding negatively charged ADP-ribose moieties (polyADP-ribosylation). This modification of a variety of nuclear proteins, including PARP proteins, histones, high mobility group proteins, topoisomerases, gyrases, DNA methyltransferase and demethylases, and the insulator protein CTCF, causes chromatin remodeling. Thus, the epigenetic effect of polyADP-ribosylation has been recently disclosed.

PARP1, the most abundant nuclear PARP protein, is activated by binding to DNA breaks, and its polyADP-ribosylation plays a major role in DNA repair. Recently, the activation of PARP proteins, including PARP1, by a variety of signal transduction mechanisms has been disclosed in a variety of cell types and in response to various types of extracellular stimulation under physiological and pathological conditions. In addition, the binding and recruitment of ADP-ribose polymers to macrodomains in proteins is implicated in the recognition, interpretation and turnover of ADP-ribose signaling.

This Special Issue aims to contribute to the current knowledge on the implication of signal-induced polyADP-ribosylation of PARP proteins and their substrates and discuss their emerging potential as therapeutic targets.

Prof. Malka Cohen-Armon
Guest Editor

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