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Mono(ADP-ribosyl)ation and poly(ADP-ribosyl)ation are posttranslational modifications evolutionarily conserved in prokaryotes and eukaryotes. They entail transfer of one or more ADP-ribose moieties from NAD+ to acceptor proteins with the simultaneous release of nicotinamide. The resultant ADP-ribosylated acceptor proteins regulate diverse cellular functions. For instance, ADP-ribosyltransferase 1 (ART1) catalyzes mono(ADP-ribosyl)ation of arginine residues in Trim72, a protein specifically expressed in muscle cells and involved in cell membrane repair, which is enhanced upon its ADP-ribosylation. By contrast, the contribution made by ADP-ribosylation to membrane repair in epithelial cells remains unclear. In this study, we investigated the involvement of ADP-ribosylation in cell membrane repair in HEK293T and HeLa cells. We found that upon induction of membrane damage using streptolysin-O, poly(ADP-ribose) polymerase 1 (PARP1) catalyzed poly(ADP-ribosyl)ation. In scratch assays, inhibition of PARP1 activity using the nonspecific PARP inhibitor PJ34 or shRNA targeting PARP1 delayed wound healing, suggesting that PARP1-catalyzed poly(ADP-ribosyl)ation plays a key role in membrane repair in epithelial cells. © 2022 Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.

Citation

Masato Mashimo, Momoko Kita, Akari Nobeyama, Atsuo Nomura, Takeshi Fujii. PARP1 is activated by membrane damage and is involved in membrane repair through poly(ADP-ribosyl)ation. Genes to cells : devoted to molecular & cellular mechanisms. 2022 Apr;27(4):305-312

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PMID: 35124853

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