ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses

Sumio Hayakawa; Souichi Shiratori; Hiroaki Yamato; Takeshi Kameyama; Chihiro Kitatsuji; Fumi Kashigi; Showhey Goto; Shoichiro Kameoka; Daisuke Fujikura; Taisho Yamada; Tatsuaki Mizutani; Mika Kazumata; Maiko Sato; Junji Tanaka; Masahiro Asaka; Yusuke Ohba; Tadaaki Miyazaki; Masahiro Imamura; Akinori Takaoka; Junji TANAKA

doi:10.1038/ni.1963

ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses

Sumio Hayakawa, Souichi Shiratori, Hiroaki Yamato, Takeshi Kameyama, Chihiro Kitatsuji, Fumi Kashigi, Showhey Goto, Shoichiro Kameoka, Daisuke Fujikura, Taisho Yamada, Tatsuaki Mizutani, Mika Kazumata, Maiko Sato, Junji Tanaka, Masahiro Asaka, Yusuke Ohba, Tadaaki Miyazaki, Masahiro Imamura, Akinori Takaoka, Junji TANAKA

Department of Human Life Sciences

Research output: Contribution to journal › Misc

Abstract

The poly(ADP-ribose) polymerases (PARPs) participate in many biological and pathological processes. Here we report that the PARP-13 shorter isoform (ZAPS), rather than the full-length protein (ZAP), was selectively induced by 5'-triphosphate-modified RNA (3pRNA) and functioned as a potent stimulator of interferon responses in human cells mediated by the RNA helicase RIG-I. ZAPS associated with RIG-I to promote the oligomerization and ATPase activity of RIG-I, which led to robust activation of IRF3 and NF-kappa B transcription factors. Disruption of the gene encoding ZAPS resulted in impaired induction of interferon-alpha (IFN-alpha), IFN-beta and other cytokines after viral infection. These results indicate that ZAPS is a key regulator of RIG-I signaling during the innate antiviral immune response, which suggests its possible use as a therapeutic target for viral control.

Translated title of the contribution	ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses
Original language	American English
Pages (from-to)	37 - U56
Journal	NATURE IMMUNOLOGY
Volume	12
Issue number	1
DOIs	https://doi.org/10.1038/ni.1963
State	Published - Jan 2011

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Sumio Hayakawa, Souichi Shiratori, Hiroaki Yamato, Takeshi Kameyama, Chihiro Kitatsuji, Fumi Kashigi, Showhey Goto, Shoichiro Kameoka, Daisuke Fujikura, Taisho Yamada, Tatsuaki Mizutani, Mika Kazumata, Maiko Sato, Junji Tanaka, Masahiro Asaka, Yusuke Ohba, Tadaaki Miyazaki, Masahiro Imamura, Akinori Takaoka, & TANAKA, J. (2011). ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses. NATURE IMMUNOLOGY, 12(1), 37 - U56. https://doi.org/10.1038/ni.1963

@article{ff07a4377d3a49f0810563766c1892fa,

title = "ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses",

abstract = "The poly(ADP-ribose) polymerases (PARPs) participate in many biological and pathological processes. Here we report that the PARP-13 shorter isoform (ZAPS), rather than the full-length protein (ZAP), was selectively induced by 5'-triphosphate-modified RNA (3pRNA) and functioned as a potent stimulator of interferon responses in human cells mediated by the RNA helicase RIG-I. ZAPS associated with RIG-I to promote the oligomerization and ATPase activity of RIG-I, which led to robust activation of IRF3 and NF-kappa B transcription factors. Disruption of the gene encoding ZAPS resulted in impaired induction of interferon-alpha (IFN-alpha), IFN-beta and other cytokines after viral infection. These results indicate that ZAPS is a key regulator of RIG-I signaling during the innate antiviral immune response, which suggests its possible use as a therapeutic target for viral control.",

author = "\{Sumio Hayakawa\} and \{Souichi Shiratori\} and \{Hiroaki Yamato\} and \{Takeshi Kameyama\} and \{Chihiro Kitatsuji\} and \{Fumi Kashigi\} and \{Showhey Goto\} and \{Shoichiro Kameoka\} and \{Daisuke Fujikura\} and \{Taisho Yamada\} and \{Tatsuaki Mizutani\} and \{Mika Kazumata\} and \{Maiko Sato\} and \{Junji Tanaka\} and \{Masahiro Asaka\} and \{Yusuke Ohba\} and \{Tadaaki Miyazaki\} and \{Masahiro Imamura\} and \{Akinori Takaoka\} and Junji TANAKA",

year = "2011",

month = jan,

doi = "10.1038/ni.1963",

language = "American English",

volume = "12",

pages = "37 -- U56",

journal = "NATURE IMMUNOLOGY",

issn = "1529-2908",

publisher = "Nature Research",

number = "1",

}

Sumio Hayakawa, Souichi Shiratori, Hiroaki Yamato, Takeshi Kameyama, Chihiro Kitatsuji, Fumi Kashigi, Showhey Goto, Shoichiro Kameoka, Daisuke Fujikura, Taisho Yamada, Tatsuaki Mizutani, Mika Kazumata, Maiko Sato, Junji Tanaka, Masahiro Asaka, Yusuke Ohba, Tadaaki Miyazaki, Masahiro Imamura, Akinori Takaoka, & TANAKA, J 2011, 'ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses', NATURE IMMUNOLOGY, vol. 12, no. 1, pp. 37 - U56. https://doi.org/10.1038/ni.1963

TY - JOUR

T1 - ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses

AU - Sumio Hayakawa, null

AU - Souichi Shiratori, null

AU - Hiroaki Yamato, null

AU - Takeshi Kameyama, null

AU - Chihiro Kitatsuji, null

AU - Fumi Kashigi, null

AU - Showhey Goto, null

AU - Shoichiro Kameoka, null

AU - Daisuke Fujikura, null

AU - Taisho Yamada, null

AU - Tatsuaki Mizutani, null

AU - Mika Kazumata, null

AU - Maiko Sato, null

AU - Junji Tanaka, null

AU - Masahiro Asaka, null

AU - Yusuke Ohba, null

AU - Tadaaki Miyazaki, null

AU - Masahiro Imamura, null

AU - Akinori Takaoka, null

AU - TANAKA, Junji

PY - 2011/1

Y1 - 2011/1

N2 - The poly(ADP-ribose) polymerases (PARPs) participate in many biological and pathological processes. Here we report that the PARP-13 shorter isoform (ZAPS), rather than the full-length protein (ZAP), was selectively induced by 5'-triphosphate-modified RNA (3pRNA) and functioned as a potent stimulator of interferon responses in human cells mediated by the RNA helicase RIG-I. ZAPS associated with RIG-I to promote the oligomerization and ATPase activity of RIG-I, which led to robust activation of IRF3 and NF-kappa B transcription factors. Disruption of the gene encoding ZAPS resulted in impaired induction of interferon-alpha (IFN-alpha), IFN-beta and other cytokines after viral infection. These results indicate that ZAPS is a key regulator of RIG-I signaling during the innate antiviral immune response, which suggests its possible use as a therapeutic target for viral control.

AB - The poly(ADP-ribose) polymerases (PARPs) participate in many biological and pathological processes. Here we report that the PARP-13 shorter isoform (ZAPS), rather than the full-length protein (ZAP), was selectively induced by 5'-triphosphate-modified RNA (3pRNA) and functioned as a potent stimulator of interferon responses in human cells mediated by the RNA helicase RIG-I. ZAPS associated with RIG-I to promote the oligomerization and ATPase activity of RIG-I, which led to robust activation of IRF3 and NF-kappa B transcription factors. Disruption of the gene encoding ZAPS resulted in impaired induction of interferon-alpha (IFN-alpha), IFN-beta and other cytokines after viral infection. These results indicate that ZAPS is a key regulator of RIG-I signaling during the innate antiviral immune response, which suggests its possible use as a therapeutic target for viral control.

U2 - 10.1038/ni.1963

DO - 10.1038/ni.1963

M3 - Misc

C2 - 21102435

SN - 1529-2908

VL - 12

SP - 37 - U56

JO - NATURE IMMUNOLOGY

JF - NATURE IMMUNOLOGY

IS - 1

ER -

ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses

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