Unknown

Dataset Information

0

K63-linked polyubiquitination of LGP2 by Riplet regulates RIG-I-dependent innate immune response


ABSTRACT: Type I interferons (IFNs) exhibit strong antiviral activity and induce the expression of antiviral proteins. Since excessive expression of type I IFNs is harmful to the host, their expression should be turned off at the appropriate time. In this study, we find that post-translational modification of LGP2, a member of the RIG-I-like receptor family, modulates antiviral innate immune responses. The LGP2 protein undergoes K63-linked polyubiquitination in response to cytoplasmic double-stranded RNAs or viral infection. Our mass spectrometry analysis reveals the K residues ubiquitinated by the Riplet ubiquitin ligase. LGP2 ubiquitination occurs with a delay compared to RIG-I ubiquitination. Interestingly, ubiquitination-defective LGP2 mutations increase the expression of type I IFN at a late phase, whereas the mutant proteins attenuate other antiviral proteins, such as SP100, PML, and ANKRD1. Our data indicate that delayed polyubiquitination of LGP2 fine-tunes RIG-I-dependent antiviral innate immune responses at a late phase of viral infection.

SUBMITTER: Dr. Takahisa Kouwaki 

PROVIDER: S-SCDT-10_15252-EMBR_202254844 | biostudies-other |

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC3738492 | biostudies-literature
| S-EPMC8137702 | biostudies-literature
| S-EPMC5520913 | biostudies-literature
| S-EPMC8315805 | biostudies-literature
| S-EPMC6901795 | biostudies-literature
| S-EPMC4436831 | biostudies-other
| S-EPMC6739404 | biostudies-literature
| S-EPMC6521028 | biostudies-literature
| S-EPMC10681309 | biostudies-literature
| S-EPMC7862670 | biostudies-literature