Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response

Abstract RIG-I and MDA5 are cytoplasmic viral RNA sensors that belong to the RIG-I-like receptors (RLRs), which induce antiviral innate immune responses, including the production of type I interferon and other pro-inflammatory cytokines. After recognition of viral RNA, the N-terminal caspase activat...

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Autores principales:	Takahisa Kouwaki, Masaaki Okamoto, Hirotake Tsukamoto, Yoshimi Fukushima, Misako Matsumoto, Tsukasa Seya, Hiroyuki Oshiumi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9be71f73eb1d49e9a5dea918b6fa101c
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spelling	oai:doaj.org-article:9be71f73eb1d49e9a5dea918b6fa101c2021-12-02T11:53:09ZZyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response10.1038/s41598-017-12224-72045-2322https://doaj.org/article/9be71f73eb1d49e9a5dea918b6fa101c2017-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-12224-7https://doaj.org/toc/2045-2322Abstract RIG-I and MDA5 are cytoplasmic viral RNA sensors that belong to the RIG-I-like receptors (RLRs), which induce antiviral innate immune responses, including the production of type I interferon and other pro-inflammatory cytokines. After recognition of viral RNA, the N-terminal caspase activation and recruitment domains (CARDs) of RIG-I and MDA5 bind to a CARD in the MAVS adaptor molecule, resulting in MAVS oligomerization and downstream signaling. To reveal the molecular mechanism of MAVS-dependent signaling, we performed a yeast two-hybrid screening and identified zyxin as a protein that binds to MAVS. Zyxin co-immunoprecipitated with MAVS in human cells. A proximity ligation assay showed that zyxin and MAVS partly co-localized on mitochondria. Ectopic expression of zyxin augmented MAVS-mediated IFN-β promoter activation, and knockdown of zyxin (ZYX) attenuated the IFN-β promoter activation. Moreover, ZYX knockdown reduced the expression of type I IFN and an interferon-inducible gene after stimulation with polyI:C or influenza A virus RNA. Interestingly, physical interactions between RLRs and MAVS were abrogated by ZYX knockdown. These observations indicate that zyxin serves as a scaffold for the interactions between RLRs and MAVS.Takahisa KouwakiMasaaki OkamotoHirotake TsukamotoYoshimi FukushimaMisako MatsumotoTsukasa SeyaHiroyuki OshiumiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Takahisa Kouwaki Masaaki Okamoto Hirotake Tsukamoto Yoshimi Fukushima Misako Matsumoto Tsukasa Seya Hiroyuki Oshiumi Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response
description	Abstract RIG-I and MDA5 are cytoplasmic viral RNA sensors that belong to the RIG-I-like receptors (RLRs), which induce antiviral innate immune responses, including the production of type I interferon and other pro-inflammatory cytokines. After recognition of viral RNA, the N-terminal caspase activation and recruitment domains (CARDs) of RIG-I and MDA5 bind to a CARD in the MAVS adaptor molecule, resulting in MAVS oligomerization and downstream signaling. To reveal the molecular mechanism of MAVS-dependent signaling, we performed a yeast two-hybrid screening and identified zyxin as a protein that binds to MAVS. Zyxin co-immunoprecipitated with MAVS in human cells. A proximity ligation assay showed that zyxin and MAVS partly co-localized on mitochondria. Ectopic expression of zyxin augmented MAVS-mediated IFN-β promoter activation, and knockdown of zyxin (ZYX) attenuated the IFN-β promoter activation. Moreover, ZYX knockdown reduced the expression of type I IFN and an interferon-inducible gene after stimulation with polyI:C or influenza A virus RNA. Interestingly, physical interactions between RLRs and MAVS were abrogated by ZYX knockdown. These observations indicate that zyxin serves as a scaffold for the interactions between RLRs and MAVS.
format	article
author	Takahisa Kouwaki Masaaki Okamoto Hirotake Tsukamoto Yoshimi Fukushima Misako Matsumoto Tsukasa Seya Hiroyuki Oshiumi
author_facet	Takahisa Kouwaki Masaaki Okamoto Hirotake Tsukamoto Yoshimi Fukushima Misako Matsumoto Tsukasa Seya Hiroyuki Oshiumi
author_sort	Takahisa Kouwaki
title	Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response
title_short	Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response
title_full	Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response
title_fullStr	Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response
title_full_unstemmed	Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response
title_sort	zyxin stabilizes rig-i and mavs interactions and promotes type i interferon response
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/9be71f73eb1d49e9a5dea918b6fa101c
work_keys_str_mv	AT takahisakouwaki zyxinstabilizesrigiandmavsinteractionsandpromotestypeiinterferonresponse AT masaakiokamoto zyxinstabilizesrigiandmavsinteractionsandpromotestypeiinterferonresponse AT hirotaketsukamoto zyxinstabilizesrigiandmavsinteractionsandpromotestypeiinterferonresponse AT yoshimifukushima zyxinstabilizesrigiandmavsinteractionsandpromotestypeiinterferonresponse AT misakomatsumoto zyxinstabilizesrigiandmavsinteractionsandpromotestypeiinterferonresponse AT tsukasaseya zyxinstabilizesrigiandmavsinteractionsandpromotestypeiinterferonresponse AT hiroyukioshiumi zyxinstabilizesrigiandmavsinteractionsandpromotestypeiinterferonresponse
_version_	1718394881469054976

Zyxin stabilizes RIG-I and MAVS interactions and promotes type I interferon response

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