2. Academic Validation
  3. PARP1 is activated by membrane damage and is involved in membrane repair through poly(ADP-ribosyl)ation

PARP1 is activated by membrane damage and is involved in membrane repair through poly(ADP-ribosyl)ation

  • Genes Cells. 2022 Apr;27(4):305-312. doi: 10.1111/gtc.12926.
Masato Mashimo 1,  Momoko Kita 1,  Akari Nobeyama 1,  Atsuo Nomura 1,  Takeshi Fujii 1
Affiliations

Affiliation

  • 1 Department of Pharmacology, Faculty of Pharmaceutical Sciences, Doshisha Women's College of Liberal Arts, Kyotanabe, Japan.
PMID: 35124853 DOI: 10.1111/gtc.12926
Abstract

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.

Keywords

ADP-ribosylation; PARP1; membrane repair.

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