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Journal article

Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity

Abstract:
ISG15 is an interferon-stimulated, ubiquitin-like protein that can conjugate to substrate proteins (ISGylation) to counteract microbial infection, but the underlying mechanisms remain elusive. Here, we use a virus-like particle trapping technology to identify ISG15-binding proteins and discover Ring Finger Protein 213 (RNF213) as an ISG15 interactor and cellular sensor of ISGylated proteins. RNF213 is a poorly characterized, interferon-induced megaprotein that is frequently mutated in Moyamoya disease, a rare cerebrovascular disorder. We report that interferon induces ISGylation and oligomerization of RNF213 on lipid droplets, where it acts as a sensor for ISGylated proteins. We show that RNF213 has broad antimicrobial activity in vitro and in vivo, counteracting infection with Listeria monocytogenes, herpes simplex virus 1, human respiratory syncytial virus and coxsackievirus B3, and we observe a striking co-localization of RNF213 with intracellular bacteria. Together, our findings provide molecular insights into the ISGylation pathway and reveal RNF213 as a key antimicrobial effector.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-021-26061-w

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Role:
Author
ORCID:
0000-0002-0007-5091
More by this author
Role:
Author
ORCID:
0000-0002-7348-0223


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
12
Issue:
1
Article number:
5772
Publication date:
2021-10-01
Acceptance date:
2021-09-14
DOI:
EISSN:
2041-1723
Pmid:
34599178


Language:
English
Keywords:
Pubs id:
1198434
Local pid:
pubs:1198434
Deposit date:
2022-01-04

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