ADP-ribosyltransferase PARP11 modulates the interferon antiviral response by mono-ADP-ribosylating the ubiquitin E3 ligase β-TrCP

Guo, Tingting; Zuo, Yibo; Qian, Liping; Liu, Jin; Yuan, Yukang; Xu, Kailin; Miao, Ying; Feng, Qian; Chen, Xiangjie; Jin, Lincong; Zhang, Liting; Dong, Chunsheng; Xiong, Sidong; Zheng, Hui

doi:10.1038/s41564-019-0428-3

Cited by 80 publications

(85 citation statements)

References 47 publications

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“…Our study found that viral infection upregulated the mRNA and protein levels of HOIP in cells 6 h after infection. It has been reported that viral infection activates two major pathways, IFN production and NF-κB activation, which mediate cellular antiviral function [30][31][32][33][34] . We found that the induction of HOIP by viruses was through the NF-κB pathway.…”

Section: Discussionmentioning

confidence: 99%

Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling

et al. 2020

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Linear ubiquitination is a critical regulator of inflammatory signaling pathways. However, linearly ubiquitinated substrates and the biological significance of linear ubiquitination is incompletely understood. Here, we show that STAT1 has linear ubiquitination at Lys511 and Lys652 residues in intact cells, which inhibits STAT1 binding to the type-I interferon receptor IFNAR2, thereby restricting STAT1 activation and resulting in type-I interferon signaling homeostasis. Linear ubiquitination of STAT1 is removed rapidly by OTULIN upon type-I interferon stimulation, which facilitates activation of interferon-STAT1 signaling. Furthermore, viruses induce HOIP expression through the NF-κB pathway, which in turn increases linear ubiquitination of STAT1 and thereby inhibits interferon antiviral response. Consequently, HOIL-1L heterozygous mice have active STAT1 signaling and enhanced responses to type-I interferons. These findings demonstrate a linear ubiquitination-mediated switch between homeostasis and activation of type-I interferon signaling, and suggest potential strategies for clinical antiviral therapy.

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Section: Discussionmentioning

confidence: 99%

Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling

et al. 2020

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“…Recently, PARP11 was shown to block IFN signaling by ADP-ribosylating the E3 ubiquitin ligase β-transducin repeat-containing protein (β-TrCP), which lead to the ubiquitination and degradation of the interferon α/β receptor (IFNAR) ( Fig. 1B; Guo et al 2019). siRNA silencing of PARP11 or treatment with rucaparib, a pan-PARP inhibitor used in advanced ovarian cancer, inhibited the replication of VSV and HSV-1.…”

Section: Other Parpsmentioning

confidence: 99%

The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions

et al. 2020

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Poly-adenosine diphosphate-ribose polymerases (PARPs) promote ADP-ribosylation, a highly conserved, fundamental posttranslational modification (PTM). PARP catalytic domains transfer the ADP-ribose moiety from NAD+ to amino acid residues of target proteins, leading to mono- or poly-ADP-ribosylation (MARylation or PARylation). This PTM regulates various key biological and pathological processes. In this review, we focus on the roles of the PARP family members in inflammation and host–pathogen interactions. Here we give an overview the current understanding of the mechanisms by which PARPs promote or suppress proinflammatory activation of macrophages, and various roles PARPs play in virus infections. We also demonstrate how innovative technologies, such as proteomics and systems biology, help to advance this research field and describe unanswered questions.

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“…h Irreversible has been suggested and so far no reversing activity has been described. Guo et al 2019;3 Feijs et al 2013;4 Bindesbøll et al 2016;5 Carter-O'Connell et al 2016;6 Vyas et al 2014;7 Carter-O'Connell et al 2018;8 Zhang et al 2013;9 Chen et al 2011;10 Jankevicius et al 2013;11 Rosenthal et al 2013;12 Sharifi et al 2013;13 Rack et al 2015;14 Yang et al 2017;15 Sauve and Youn 2012;16 Peterson et al 2011;17 Ono et al 2006;18 Bonfiglio et al 2017;19 Leidecker et al 2016;20 Leslie Pedrioli et al 2018;21 Bartlett et al 2018;22 Palazzo et al 2018;23 Fontana et al 2017;24 Abplanalp et al 2017;25 D'Amours et al 1999;26 Rippmann et al 2002;27 Brochu et al 1994;28 Barkauskaite et al 2013;29 Oka et al 2006;30 Munnur et al 2019;31 Munir et al 2018b;32 Talhaoui et al 2016;33 Munnur and Ahel 2017;34 Munir et al 2018a;35 Banerjee et al 2019;…”

Section: Beyond Ptms: Adp-ribosylation Of Nucleic Acidsunclassified

(ADP-ribosyl)hydrolases: structure, function, and biology

2020

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ADP-ribosylation is an intricate and versatile posttranslational modification involved in the regulation of a vast variety of cellular processes in all kingdoms of life. Its complexity derives from the varied range of different chemical linkages, including to several amino acid side chains as well as nucleic acids termini and bases, it can adopt. In this review, we provide an overview of the different families of (ADP-ribosyl)hydrolases. We discuss their molecular functions, physiological roles, and influence on human health and disease. Together, the accumulated data support the increasingly compelling view that (ADP-ribosyl)hydrolases are a vital element within ADP-ribosyl signaling pathways and they hold the potential for novel therapeutic approaches as well as a deeper understanding of ADP-ribosylation as a whole.

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ADP-ribosyltransferase PARP11 modulates the interferon antiviral response by mono-ADP-ribosylating the ubiquitin E3 ligase β-TrCP

Cited by 80 publications

References 47 publications

Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling

Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling

The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions

(ADP-ribosyl)hydrolases: structure, function, and biology

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