PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation

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PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation. / Kar, Pulak; Chatrin, Chatrin; Đukić, Nina; Suyari, Osamu; Schuller, Marion; Zhu, Kang; Prokhorova, Evgeniia; Bigot, Nicolas; Ahel, Juraj; Elsborg, Jonas Damgaard; Nielsen, Michael L; Clausen, Tim; Huet, Sébastien; Niepel, Mario; Sanyal, Sumana; Ahel, Dragana; Smith, Rebecca; Ahel, Ivan.

In: EMBO Journal, Vol. 43, No. 14, 2024, p. 2929-2953.

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

Harvard

Kar, P, Chatrin, C, Đukić, N, Suyari, O, Schuller, M, Zhu, K, Prokhorova, E, Bigot, N, Ahel, J, Elsborg, JD, Nielsen, ML, Clausen, T, Huet, S, Niepel, M, Sanyal, S, Ahel, D, Smith, R & Ahel, I 2024, 'PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation', EMBO Journal, vol. 43, no. 14, pp. 2929-2953. https://doi.org/10.1038/s44318-024-00126-0

APA

Kar, P., Chatrin, C., Đukić, N., Suyari, O., Schuller, M., Zhu, K., Prokhorova, E., Bigot, N., Ahel, J., Elsborg, J. D., Nielsen, M. L., Clausen, T., Huet, S., Niepel, M., Sanyal, S., Ahel, D., Smith, R., & Ahel, I. (2024). PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation. EMBO Journal, 43(14), 2929-2953. https://doi.org/10.1038/s44318-024-00126-0

Vancouver

Kar P, Chatrin C, Đukić N, Suyari O, Schuller M, Zhu K et al. PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation. EMBO Journal. 2024;43(14):2929-2953. https://doi.org/10.1038/s44318-024-00126-0

Author

Kar, Pulak ; Chatrin, Chatrin ; Đukić, Nina ; Suyari, Osamu ; Schuller, Marion ; Zhu, Kang ; Prokhorova, Evgeniia ; Bigot, Nicolas ; Ahel, Juraj ; Elsborg, Jonas Damgaard ; Nielsen, Michael L ; Clausen, Tim ; Huet, Sébastien ; Niepel, Mario ; Sanyal, Sumana ; Ahel, Dragana ; Smith, Rebecca ; Ahel, Ivan. / PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation. In: EMBO Journal. 2024 ; Vol. 43, No. 14. pp. 2929-2953.

Bibtex

@article{c919ad1ae3284fd895ea9cab0e6d72a6,
title = "PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation",
abstract = "PARP-catalysed ADP-ribosylation (ADPr) is important in regulating various cellular pathways. Until recently, PARP-dependent mono-ADP-ribosylation has been poorly understood due to the lack of sensitive detection methods. Here, we utilised an improved antibody to detect mono-ADP-ribosylation. We visualised endogenous interferon (IFN)-induced ADP-ribosylation and show that PARP14 is a major enzyme responsible for this modification. Fittingly, this signalling is reversed by the macrodomain from SARS-CoV-2 (Mac1), providing a possible mechanism by which Mac1 counteracts the activity of antiviral PARPs. Our data also elucidate a major role of PARP9 and its binding partner, the E3 ubiquitin ligase DTX3L, in regulating PARP14 activity through protein-protein interactions and by the hydrolytic activity of PARP9 macrodomain 1. Finally, we also present the first visualisation of ADPr-dependent ubiquitylation in the IFN response. These approaches should further advance our understanding of IFN-induced ADPr and ubiquitin signalling processes and could shed light on how different pathogens avoid such defence pathways.",
keywords = "ADP-ribosylation, Immune Response, Interferon Response, SARS-CoV2, Ubiquitin",
author = "Pulak Kar and Chatrin Chatrin and Nina {\D}uki{\'c} and Osamu Suyari and Marion Schuller and Kang Zhu and Evgeniia Prokhorova and Nicolas Bigot and Juraj Ahel and Elsborg, {Jonas Damgaard} and Nielsen, {Michael L} and Tim Clausen and S{\'e}bastien Huet and Mario Niepel and Sumana Sanyal and Dragana Ahel and Rebecca Smith and Ivan Ahel",
note = "Publisher Copyright: {\textcopyright} The Author(s) 2024.",
year = "2024",
doi = "10.1038/s44318-024-00126-0",
language = "English",
volume = "43",
pages = "2929--2953",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "14",

}

RIS

TY - JOUR

T1 - PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation

AU - Kar, Pulak

AU - Chatrin, Chatrin

AU - Đukić, Nina

AU - Suyari, Osamu

AU - Schuller, Marion

AU - Zhu, Kang

AU - Prokhorova, Evgeniia

AU - Bigot, Nicolas

AU - Ahel, Juraj

AU - Elsborg, Jonas Damgaard

AU - Nielsen, Michael L

AU - Clausen, Tim

AU - Huet, Sébastien

AU - Niepel, Mario

AU - Sanyal, Sumana

AU - Ahel, Dragana

AU - Smith, Rebecca

AU - Ahel, Ivan

N1 - Publisher Copyright: © The Author(s) 2024.

PY - 2024

Y1 - 2024

N2 - PARP-catalysed ADP-ribosylation (ADPr) is important in regulating various cellular pathways. Until recently, PARP-dependent mono-ADP-ribosylation has been poorly understood due to the lack of sensitive detection methods. Here, we utilised an improved antibody to detect mono-ADP-ribosylation. We visualised endogenous interferon (IFN)-induced ADP-ribosylation and show that PARP14 is a major enzyme responsible for this modification. Fittingly, this signalling is reversed by the macrodomain from SARS-CoV-2 (Mac1), providing a possible mechanism by which Mac1 counteracts the activity of antiviral PARPs. Our data also elucidate a major role of PARP9 and its binding partner, the E3 ubiquitin ligase DTX3L, in regulating PARP14 activity through protein-protein interactions and by the hydrolytic activity of PARP9 macrodomain 1. Finally, we also present the first visualisation of ADPr-dependent ubiquitylation in the IFN response. These approaches should further advance our understanding of IFN-induced ADPr and ubiquitin signalling processes and could shed light on how different pathogens avoid such defence pathways.

AB - PARP-catalysed ADP-ribosylation (ADPr) is important in regulating various cellular pathways. Until recently, PARP-dependent mono-ADP-ribosylation has been poorly understood due to the lack of sensitive detection methods. Here, we utilised an improved antibody to detect mono-ADP-ribosylation. We visualised endogenous interferon (IFN)-induced ADP-ribosylation and show that PARP14 is a major enzyme responsible for this modification. Fittingly, this signalling is reversed by the macrodomain from SARS-CoV-2 (Mac1), providing a possible mechanism by which Mac1 counteracts the activity of antiviral PARPs. Our data also elucidate a major role of PARP9 and its binding partner, the E3 ubiquitin ligase DTX3L, in regulating PARP14 activity through protein-protein interactions and by the hydrolytic activity of PARP9 macrodomain 1. Finally, we also present the first visualisation of ADPr-dependent ubiquitylation in the IFN response. These approaches should further advance our understanding of IFN-induced ADPr and ubiquitin signalling processes and could shed light on how different pathogens avoid such defence pathways.

KW - ADP-ribosylation

KW - Immune Response

KW - Interferon Response

KW - SARS-CoV2

KW - Ubiquitin

U2 - 10.1038/s44318-024-00126-0

DO - 10.1038/s44318-024-00126-0

M3 - Journal article

C2 - 38834853

AN - SCOPUS:85195164250

VL - 43

SP - 2929

EP - 2953

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 14

ER -

ID: 394714476