PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities. / Đukić, Nina; Strømland, Øyvind; Elsborg, Jonas Damgaard; Munnur, Deeksha; Zhu, Kang; Schuller, Marion; Chatrin, Chatrin; Kar, Pulak; Duma, Lena; Suyari, Osamu; Rack, Johannes Gregor Matthias; Baretić, Domagoj; Crudgington, Dorian Richard Kenneth; Groslambert, Joséphine; Fowler, Gerissa; Wijngaarden, Sven; Prokhorova, Evgeniia; Rehwinkel, Jan; Schüler, Herwig; Filippov, Dmitri V.; Sanyal, Sumana; Ahel, Dragana; Nielsen, Michael L.; Smith, Rebecca; Ahel, Ivan.

In: Science Advances, Vol. 9, No. 37, eadi2687, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Đukić, N, Strømland, Ø, Elsborg, JD, Munnur, D, Zhu, K, Schuller, M, Chatrin, C, Kar, P, Duma, L, Suyari, O, Rack, JGM, Baretić, D, Crudgington, DRK, Groslambert, J, Fowler, G, Wijngaarden, S, Prokhorova, E, Rehwinkel, J, Schüler, H, Filippov, DV, Sanyal, S, Ahel, D, Nielsen, ML, Smith, R & Ahel, I 2023, 'PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities', Science Advances, vol. 9, no. 37, eadi2687. https://doi.org/10.1126/sciadv.adi2687

APA

Đukić, N., Strømland, Ø., Elsborg, J. D., Munnur, D., Zhu, K., Schuller, M., Chatrin, C., Kar, P., Duma, L., Suyari, O., Rack, J. G. M., Baretić, D., Crudgington, D. R. K., Groslambert, J., Fowler, G., Wijngaarden, S., Prokhorova, E., Rehwinkel, J., Schüler, H., ... Ahel, I. (2023). PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities. Science Advances, 9(37), [eadi2687]. https://doi.org/10.1126/sciadv.adi2687

Vancouver

Đukić N, Strømland Ø, Elsborg JD, Munnur D, Zhu K, Schuller M et al. PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities. Science Advances. 2023;9(37). eadi2687. https://doi.org/10.1126/sciadv.adi2687

Author

Đukić, Nina ; Strømland, Øyvind ; Elsborg, Jonas Damgaard ; Munnur, Deeksha ; Zhu, Kang ; Schuller, Marion ; Chatrin, Chatrin ; Kar, Pulak ; Duma, Lena ; Suyari, Osamu ; Rack, Johannes Gregor Matthias ; Baretić, Domagoj ; Crudgington, Dorian Richard Kenneth ; Groslambert, Joséphine ; Fowler, Gerissa ; Wijngaarden, Sven ; Prokhorova, Evgeniia ; Rehwinkel, Jan ; Schüler, Herwig ; Filippov, Dmitri V. ; Sanyal, Sumana ; Ahel, Dragana ; Nielsen, Michael L. ; Smith, Rebecca ; Ahel, Ivan. / PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities. In: Science Advances. 2023 ; Vol. 9, No. 37.

Bibtex

@article{388a77702a2649c1b3f2dfa51129d116,
title = "PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities",
abstract = "PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription, and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. We show that PARP14 is a dual-function enzyme with both ADP-ribosyl transferase and hydrolase activity acting on both protein and nucleic acid substrates. In particular, we show that the PARP14 macrodomain 1 is an active ADP-ribosyl hydrolase. We also demonstrate hydrolytic activity for the first macrodomain of PARP9. We reveal that expression of a PARP14 mutant with the inactivated macrodomain 1 results in a marked increase in mono(ADP-ribosyl)ation of proteins in human cells, including PARP14 itself and antiviral PARP13, and displays specific cellular phenotypes. Moreover, we demonstrate that the closely related hydrolytically active macrodomain of SARS2 Nsp3, Mac1, efficiently reverses PARP14 ADP-ribosylation in vitro and in cells, supporting the evolution of viral macrodomains to counteract PARP14-mediated antiviral response.",
author = "Nina {\D}uki{\'c} and {\O}yvind Str{\o}mland and Elsborg, {Jonas Damgaard} and Deeksha Munnur and Kang Zhu and Marion Schuller and Chatrin Chatrin and Pulak Kar and Lena Duma and Osamu Suyari and Rack, {Johannes Gregor Matthias} and Domagoj Bareti{\'c} and Crudgington, {Dorian Richard Kenneth} and Jos{\'e}phine Groslambert and Gerissa Fowler and Sven Wijngaarden and Evgeniia Prokhorova and Jan Rehwinkel and Herwig Sch{\"u}ler and Filippov, {Dmitri V.} and Sumana Sanyal and Dragana Ahel and Nielsen, {Michael L.} and Rebecca Smith and Ivan Ahel",
year = "2023",
doi = "10.1126/sciadv.adi2687",
language = "English",
volume = "9",
journal = "Science advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "37",

}

RIS

TY - JOUR

T1 - PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities

AU - Đukić, Nina

AU - Strømland, Øyvind

AU - Elsborg, Jonas Damgaard

AU - Munnur, Deeksha

AU - Zhu, Kang

AU - Schuller, Marion

AU - Chatrin, Chatrin

AU - Kar, Pulak

AU - Duma, Lena

AU - Suyari, Osamu

AU - Rack, Johannes Gregor Matthias

AU - Baretić, Domagoj

AU - Crudgington, Dorian Richard Kenneth

AU - Groslambert, Joséphine

AU - Fowler, Gerissa

AU - Wijngaarden, Sven

AU - Prokhorova, Evgeniia

AU - Rehwinkel, Jan

AU - Schüler, Herwig

AU - Filippov, Dmitri V.

AU - Sanyal, Sumana

AU - Ahel, Dragana

AU - Nielsen, Michael L.

AU - Smith, Rebecca

AU - Ahel, Ivan

PY - 2023

Y1 - 2023

N2 - PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription, and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. We show that PARP14 is a dual-function enzyme with both ADP-ribosyl transferase and hydrolase activity acting on both protein and nucleic acid substrates. In particular, we show that the PARP14 macrodomain 1 is an active ADP-ribosyl hydrolase. We also demonstrate hydrolytic activity for the first macrodomain of PARP9. We reveal that expression of a PARP14 mutant with the inactivated macrodomain 1 results in a marked increase in mono(ADP-ribosyl)ation of proteins in human cells, including PARP14 itself and antiviral PARP13, and displays specific cellular phenotypes. Moreover, we demonstrate that the closely related hydrolytically active macrodomain of SARS2 Nsp3, Mac1, efficiently reverses PARP14 ADP-ribosylation in vitro and in cells, supporting the evolution of viral macrodomains to counteract PARP14-mediated antiviral response.

AB - PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription, and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. We show that PARP14 is a dual-function enzyme with both ADP-ribosyl transferase and hydrolase activity acting on both protein and nucleic acid substrates. In particular, we show that the PARP14 macrodomain 1 is an active ADP-ribosyl hydrolase. We also demonstrate hydrolytic activity for the first macrodomain of PARP9. We reveal that expression of a PARP14 mutant with the inactivated macrodomain 1 results in a marked increase in mono(ADP-ribosyl)ation of proteins in human cells, including PARP14 itself and antiviral PARP13, and displays specific cellular phenotypes. Moreover, we demonstrate that the closely related hydrolytically active macrodomain of SARS2 Nsp3, Mac1, efficiently reverses PARP14 ADP-ribosylation in vitro and in cells, supporting the evolution of viral macrodomains to counteract PARP14-mediated antiviral response.

U2 - 10.1126/sciadv.adi2687

DO - 10.1126/sciadv.adi2687

M3 - Journal article

C2 - 37703374

AN - SCOPUS:85171240255

VL - 9

JO - Science advances

JF - Science advances

SN - 2375-2548

IS - 37

M1 - eadi2687

ER -

ID: 368253380