The mitochondrial ubiquitin ligase MARCH5 resolves MAVS aggregates during antiviral signalling View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-12

AUTHORS

Young-Suk Yoo, Yong-Yea Park, Jae-Hoon Kim, Hyeseon Cho, Song-Hee Kim, Ho-Soo Lee, Tae-Hwan Kim, You Sun Kim, Youngsoo Lee, Chul-Joong Kim, Jae U Jung, Jong-Soo Lee, Hyeseong Cho

ABSTRACT

Mitochondria serve as platforms for innate immunity. The mitochondrial antiviral signalling (MAVS) protein forms aggregates that elicit robust type-I interferon induction on viral infection, but persistent MAVS signalling leads to host immunopathology; it remains unknown how these signalling aggregates are resolved. Here we identify the mitochondria-resident E3 ligase, MARCH5, as a negative regulator of MAVS aggregates. March5(+/-) mice and MARCH5-deficient immune cells exhibit low viral replication and elevated type-I interferon responses to RNA viruses. MARCH5 binds MAVS only during viral stimulation when MAVS forms aggregates, and these interactions require the RING domain of MARCH5 and the CARD domain of MAVS. MARCH5, but not its RING mutant (MARCH5(H43W)), reduces the level of MAVS aggregates. MARCH5 transfers ubiquitin to Lys7 and Lys500 of MAVS and promotes its proteasome-mediated degradation. Our results indicate that MARCH5 modulates MAVS-mediated antiviral signalling, preventing excessive immune reactions. More... »

PAGES

7910

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms8910

DOI

http://dx.doi.org/10.1038/ncomms8910

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041044591

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26246171


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