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PARP11

Official Full Name
poly(ADP-ribose) polymerase family member 11
Organism
Homo sapiens
GeneID
57097
Background
Enables NAD+-protein poly-ADP-ribosyltransferase activity. Involved in protein auto-ADP-ribosylation. Located in cytosol; nuclear body; and nuclear envelope. [provided by Alliance of Genome Resources, Feb 2025]
Synonyms
ARTD11; MIB006; C12orf6;

Detailed Information

Interferon antiviral response can be modulated by PARP11 via ribosylation of the ubiquitin E3 ligase β-Trcp

Viral infections outbreak is regarded as a global health burden. Even though type I interferon (IFN-I) has a broad-spectrum antiviral effect, the virus may also exert restriction on its antiviral efficacy in host cells. How to augment the antiviral efficacy of IFN-1 remains to be elusive. In recent studies, ADP-ribosyltransferase poly (ADP-ribose) polymerase family member 11 (PARP11) was identified as a potent regulator of IFN-1 anti-viral efficacy. In vesicular stomatitis virus or Sendai virus produced IFN-1, PARP11 does not exert any restrictions, but inhibits the strength of IFN-I-activated signaling. Mechanistically, Mono-ADP-ribosylation of the ubiquitin E3 ligase β-transducin repeat-containing protein (β-Trcp) induced by the PARP11 can promote IFNα/β receptor subunit 1 (IFNAR1) ubiquitination and degradation. More than this, virus infections, like vesicular stomatitis virus, herpes simplex virus-1 and influenza A virus, can upregulate the PARP11 expression to promote ADP-ribosylation-mediated viral evasion. PARP11 inhibitor can stabilize IFNAR1, thus enhancing IFN-1 signaling and the host antiviral response. The consequence of this enhancement rendered by PARP11 inhibitor makes mice more resistant to viral infection.

Research on PARP-mediated ADP-ribosylation modifications indicated that ubiquitination of this protein may arise from the ADP-ribosylation of a protein. The poly (ADP-ribose) of ADP-ribosylated proteins has direct interactions with RNF146, which mediates ubiquitination of these ADP-ribosylated proteins. Ubiquitin E3 ligase Iduna recruitment of the ADP-ribosylated PARP1 can induce PARP1 ubiquitination, which can be also escaped from IFNAR1 recruitment of the ADP-ribosylated ubiquitin E3 ligase-β-TrCP. In total, IFN-I signaling and antiviral activity are negatively regulated by PARP11 mainly through targeting β-TrCP and degrading IFNAR1. Based on the classification of PARP11-activated signalling pathway and ADP-ribosylation as critical regulator of the IFN signalling pathway and antiviral activity, the fact of PARP inhibitor can block IFNAR1 downregulation and therefore enhances the IFN antiviral response, PARP11 can be regarded as a highly effective target for IFN antiviral efficacy improvement.

Figure 1. PARP1 and PARP11-induced MARylation of the beta-transducin repeat-containing protein (beta-TrCP). Figure 1. PARP1 and PARP11-induced MARylation of the β-transducin repeat-containing protein (β-TrCP). (Mar, et al. 2021)

References:

  1. Malgras M, Garcia M, Jousselin C, et al. The antiviral activities of poly-ADP-ribose polymerases. Viruses, 2021, 13(4): 582.
  2. Guo T, Zuo Y, Qian L, et al. ADP-ribosyltransferase PARP11 modulates the interferon antiviral response by mono-ADP-ribosylating the ubiquitin E3 ligase β-TrCP. Nature microbiology, 2019, 4(11): 1872-1884.
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