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

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‐ribosy...

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Bibliographic Details
Published in:Genes to cells : devoted to molecular & cellular mechanisms 2022-04, Vol.27 (4), p.305-312
Main Authors: Mashimo, Masato, Kita, Momoko, Nobeyama, Akari, Nomura, Atsuo, Fujii, Takeshi
Format: Article
Language:English
Subjects:
ADP‐ribosylation
Cell membranes
Epithelial cells
HEK293 Cells
HeLa Cells
Humans
membrane repair
NAD
PARP1
Poly (ADP-Ribose) Polymerase-1 - genetics
Poly (ADP-Ribose) Polymerase-1 - metabolism
Poly Adenosine Diphosphate Ribose - metabolism
Poly ADP Ribosylation
Poly(ADP-ribose) polymerase
Poly(ADP-ribose) Polymerase 1
Poly(ADP-ribose) Polymerases - chemistry
Poly(ADP-ribose) Polymerases - genetics
Poly(ADP-ribose) Polymerases - metabolism
Prokaryotes
Ribose
Ribosylation
Wound healing
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Summary: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. Upon membrane damage, PARP1 generates poly(ADP‐ribose) (PAR), involved in membrane repair.
ISSN:1356-9597
1365-2443
DOI:10.1111/gtc.12926