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PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation.
Kar, Pulak; Chatrin, Chatrin; Dukic, Nina; Suyari, Osamu; Schuller, Marion; Zhu, Kang; Prokhorova, Evgeniia; Bigot, Nicolas; Baretic, Domagoj; Ahel, Juraj; Elsborg, Jonas Damgaard; Nielsen, Michael L; Clausen, Tim; Huet, Sébastien; Niepel, Mario; Sanyal, Sumana; Ahel, Dragana; Smith, Rebecca; Ahel, Ivan.
Afiliación
  • Kar P; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Chatrin C; Department of Biological Sciences, SRM University-AP, Amaravati, 522502, India.
  • Dukic N; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Suyari O; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Schuller M; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Zhu K; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Prokhorova E; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Bigot N; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Baretic D; Univ Rennes, CNRS, IGDR (Institut de génétique et développement de Rennes) - UMR 6290, BIOSIT - UMS3480, F-35000, Rennes, France.
  • Ahel J; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Elsborg JD; Research Institute of Molecular Pathology (IMP), Vienna BioCenter, Vienna, Austria.
  • Nielsen ML; Proteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200, Copenhagen, Denmark.
  • Clausen T; Proteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200, Copenhagen, Denmark.
  • Huet S; Research Institute of Molecular Pathology (IMP), Vienna BioCenter, Vienna, Austria.
  • Niepel M; Medical University of Vienna, Vienna, Austria.
  • Sanyal S; Univ Rennes, CNRS, IGDR (Institut de génétique et développement de Rennes) - UMR 6290, BIOSIT - UMS3480, F-35000, Rennes, France.
  • Ahel D; Ribon Therapeutics, Cambridge, MA, 02140, USA.
  • Smith R; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
  • Ahel I; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
EMBO J ; 43(14): 2929-2953, 2024 Jul.
Article en En | MEDLINE | ID: mdl-38834853
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Interferones / Poli(ADP-Ribosa) Polimerasas / Ubiquitina-Proteína Ligasas / ADP-Ribosilación Límite: Humans Idioma: En Revista: EMBO J Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Interferones / Poli(ADP-Ribosa) Polimerasas / Ubiquitina-Proteína Ligasas / ADP-Ribosilación Límite: Humans Idioma: En Revista: EMBO J Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido