The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
26 08 2022
26 08 2022
Historique:
received:
23
06
2021
accepted:
10
08
2022
entrez:
26
8
2022
pubmed:
27
8
2022
medline:
31
8
2022
Statut:
epublish
Résumé
The signaling adaptor MAVS forms prion-like aggregates to activate the innate antiviral immune response after viral infection. However, spontaneous aggregation of MAVS can lead to autoimmune diseases. The molecular mechanism that prevents MAVS from spontaneous aggregation in resting cells has been enigmatic. Here we report that protein arginine methyltransferase 9 targets MAVS directly and catalyzes the arginine methylation of MAVS at the Arg41 and Arg43. In the resting state, this modification inhibits MAVS aggregation and autoactivation of MAVS. Upon virus infection, PRMT9 dissociates from the mitochondria, leading to the aggregation and activation of MAVS. Our study implicates a form of post-translational modification on MAVS, which can keep MAVS inactive in physiological conditions to maintain innate immune homeostasis.
Identifiants
pubmed: 36028484
doi: 10.1038/s41467-022-32628-y
pii: 10.1038/s41467-022-32628-y
pmc: PMC9418238
doi:
Substances chimiques
Adaptor Proteins, Signal Transducing
0
F-Box Proteins
0
MAVS protein, human
0
FBXO11 protein, human
EC 2.1.1.319
Protein-Arginine N-Methyltransferases
EC 2.1.1.319
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5016Informations de copyright
© 2022. The Author(s).
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