PARP1 is activated by membrane damage and is involved in membrane repair through poly(ADP-ribosyl)ation.
Masato MashimoMomoko KitaAkari NobeyamaAtsuo NomuraTakeshi FujiiPublished in: Genes to cells : devoted to molecular & cellular mechanisms (2022)
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.
Keyphrases
- dna damage
- dna repair
- induced apoptosis
- oxidative stress
- nitric oxide
- cell cycle arrest
- wound healing
- small molecule
- signaling pathway
- cell proliferation
- hiv infected
- cell death
- mass spectrometry
- high resolution
- high throughput
- endoplasmic reticulum stress
- high speed
- antiretroviral therapy
- atomic force microscopy
- energy transfer