Poly(ADP-Ribosyl) Code Functions

Overview

Journal Acta Naturae

Specialty Biology

Date 2021 Aug 11

PMID 34377556

Citations 5

Authors

N V Maluchenko

D O Koshkina

A V Feofanov

V M Studitsky

M P Kirpichnikov

Affiliations

Soon will be listed here.

Abstract

Poly(ADP-ribosyl)ation plays a key role in cellular metabolism. Covalent poly(ADP-ribosyl)ation affects the activity of the proteins engaged in DNA repair, chromatin structure regulation, gene expression, RNA processing, ribosome biogenesis, and protein translation. Non-covalent PAR-dependent interactions are involved in the various types of cellular response to stress and viral infection, such as inflammation, hormonal signaling, and the immune response. The review discusses how structurally different poly(ADP-ribose) (PAR) molecules composed of identical monomers can differentially participate in various cellular processes acting as the so-called "PAR code." The article describes the ability of PAR polymers to form functional biomolecular clusters through a phase-separation in response to various signals. This phase-separation contributes to rapid spatial segregation of biochemical processes and effective recruitment of the necessary components. The cellular PAR level is tightly controlled by a network of regulatory proteins: PAR code writers, readers, and erasers. Impaired PAR metabolism is associated with the development of pathological processes causing oncological, cardiovascular, and neurodegenerative diseases. Pharmacological correction of the PAR level may represent a new approach to the treatment of various diseases.

Citing Articles

Poly ADP-Ribosylation in a Plant Pathogenic Oomycete : A Key Controller of Growth and Host Plant Colonisation.

Samarskaya V, Koblova S, Suprunova T, Rogozhin E, Spechenkova N, Yakunina S J Fungi (Basel). 2025; 11(1).

PMID: 39852448 PMC: 11766942. DOI: 10.3390/jof11010029.

Disruption of Poly(ADP-ribosyl)ation Improves Plant Tolerance to Methyl Viologen-Mediated Oxidative Stress via Induction of ROS Scavenging Enzymes.

Kalinina N, Spechenkova N, Ilina I, Samarskaya V, Bagdasarova P, Zavriev S Int J Mol Sci. 2024; 25(17).

PMID: 39273315 PMC: 11395660. DOI: 10.3390/ijms25179367.

Overexpression of the WWE domain of RNF146 modulates poly-(ADP)-ribose dynamics at sites of DNA damage.

Al-Rahahleh R, Saville K, Andrews J, Wu Z, Koczor C, Sobol R bioRxiv. 2024; .

PMID: 38234836 PMC: 10793466. DOI: 10.1101/2023.12.29.573650.

ADP-Ribosylation and Antiviral Resistance in Plants.

Spechenkova N, Kalinina N, Zavriev S, Love A, Taliansky M Viruses. 2023; 15(1).

PMID: 36680280 PMC: 9861866. DOI: 10.3390/v15010241.

Poly(ADP-ribose) in Condensates: The PARtnership of Phase Separation and Site-Specific Interactions.

Alemasova E, Lavrik O Int J Mol Sci. 2022; 23(22).

PMID: 36430551 PMC: 9694962. DOI: 10.3390/ijms232214075.

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