DYRK2 Negatively Regulates Type I Interferon Induction by Promoting TBK1 Degradation via Ser527 Phosphorylation

Viral infection activates the transcription factors NF-κB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral responses. Protein kinases play a critical role in various signaling pathways by phosphorylating their substrates. Here, we identified dual-specif...

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Bibliographic Details
Published inPLoS pathogens Vol. 11; no. 9; p. e1005179
Main Authors An, Tai, Li, Shu, Pan, Wei, Tien, Po, Zhong, Bo, Shu, Hong-Bing, Wu, Shuwen
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 01.09.2015
Public Library of Science (PLoS)
Subjects
Animals
Cytokines
Deoxyribonucleic acid
DNA
Dyrk Kinases
Enzyme-Linked Immunosorbent Assay
Health aspects
HEK293 Cells
HeLa Cells
Host-virus relationships
Humans
Immunoblotting
Immunoprecipitation
Infections
Interferon
Interferon Type I - biosynthesis
Interferon Type I - immunology
Kinases
Molecular Sequence Data
Observations
Phosphorylation
Plasmids
Polymerase Chain Reaction
Protein kinases
Protein Serine-Threonine Kinases - immunology
Protein Serine-Threonine Kinases - metabolism
Protein-Tyrosine Kinases - immunology
Protein-Tyrosine Kinases - metabolism
Regulation
RNA polymerase
RNA, Small Interfering
Serine - immunology
Serine - metabolism
Signal Transduction - immunology
Transcription factors
Transduction, Genetic
Viral infections
Virus Diseases - immunology
Virus Diseases - metabolism
Online AccessGet full text

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Abstract Viral infection activates the transcription factors NF-κB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral responses. Protein kinases play a critical role in various signaling pathways by phosphorylating their substrates. Here, we identified dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) as a negative regulator of virus-triggered type I IFN induction. DYRK2 inhibited the virus-triggered induction of type I IFNs and promoted the K48-linked ubiquitination and degradation of TANK-binding kinase 1 (TBK1) in a kinase-activity-dependent manner. We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. These findings suggest that DYRK2 negatively regulates virus-triggered signaling by targeting TBK1 for phosphorylation and priming it for degradation, and these data provide new insights into the molecular mechanisms that dictate the cellular antiviral response.
AbstractList Viral infection activates the transcription factors NF-κB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral responses. Protein kinases play a critical role in various signaling pathways by phosphorylating their substrates. Here, we identified dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) as a negative regulator of virus-triggered type I IFN induction. DYRK2 inhibited the virus-triggered induction of type I IFNs and promoted the K48-linked ubiquitination and degradation of TANK-binding kinase 1 (TBK1) in a kinase-activity-dependent manner. We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. These findings suggest that DYRK2 negatively regulates virus-triggered signaling by targeting TBK1 for phosphorylation and priming it for degradation, and these data provide new insights into the molecular mechanisms that dictate the cellular antiviral response.
Viral infection activates the transcription factors NF-κB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral responses. Protein kinases play a critical role in various signaling pathways by phosphorylating their substrates. Here, we identified dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) as a negative regulator of virus-triggered type I IFN induction. DYRK2 inhibited the virus-triggered induction of type I IFNs and promoted the K48-linked ubiquitination and degradation of TANK-binding kinase 1 (TBK1) in a kinase-activity-dependent manner. We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. These findings suggest that DYRK2 negatively regulates virus-triggered signaling by targeting TBK1 for phosphorylation and priming it for degradation, and these data provide new insights into the molecular mechanisms that dictate the cellular antiviral response.Viral infection activates the transcription factors NF-κB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral responses. Protein kinases play a critical role in various signaling pathways by phosphorylating their substrates. Here, we identified dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) as a negative regulator of virus-triggered type I IFN induction. DYRK2 inhibited the virus-triggered induction of type I IFNs and promoted the K48-linked ubiquitination and degradation of TANK-binding kinase 1 (TBK1) in a kinase-activity-dependent manner. We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. These findings suggest that DYRK2 negatively regulates virus-triggered signaling by targeting TBK1 for phosphorylation and priming it for degradation, and these data provide new insights into the molecular mechanisms that dictate the cellular antiviral response.
  Viral infection activates the transcription factors NF-KB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral responses. Protein kinases play a critical role in various signaling pathways by phosphorylating their substrates. Here, we identified dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) as a negative regulator of virus-triggered type I IFN induction. DYRK2 inhibited the virus-triggered induction of type I IFNs and promoted the K48-linked ubiquitination and degradation of TANK-binding kinase 1 (TBK1) in a kinase-activity-dependent manner. We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. These findings suggest that DYRK2 negatively regulates virus-triggered signaling by targeting TBK1 for phosphorylation and priming it for degradation, and these data provide new insights into the molecular mechanisms that dictate the cellular antiviral response.
Viral infection activates the transcription factors NF-κB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral responses. Protein kinases play a critical role in various signaling pathways by phosphorylating their substrates. Here, we identified dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) as a negative regulator of virus-triggered type I IFN induction. DYRK2 inhibited the virus-triggered induction of type I IFNs and promoted the K48-linked ubiquitination and degradation of TANK-binding kinase 1 (TBK1) in a kinase-activity-dependent manner. We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. These findings suggest that DYRK2 negatively regulates virus-triggered signaling by targeting TBK1 for phosphorylation and priming it for degradation, and these data provide new insights into the molecular mechanisms that dictate the cellular antiviral response. In recent years, the mechanisms of innate antiviral immune responses mediated by pattern recognition receptors (PRRs) have been heavily investigated. All PRRs require the key molecule TANK-binding kinase 1 (TBK1) to activate the transcription factor IRF3, which leads to type I interferon induction and the cellular antiviral response. Here, we identified the dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) as a negative regulator of TBK1. DYRK2 inhibited the virus-triggered induction of type I interferon and promoted K48-linked ubiquitination and the degradation of TBK1 in a manner that depended on its kinase activity. We further found that DYRK2 phosphorylated Ser527 of TBK1, which is essential for the recruitment of NLRP4 and for the E3 ubiquitin ligase DTX4 to degrade TBK1. Our findings suggest that DYRK2 plays an important role in innate immune responses to viruses by modulating TBK1 activity and provide important insights into the intricate regulatory mechanisms of the innate immune response against viruses.
Audience Academic
Author Pan, Wei
Shu, Hong-Bing
Wu, Shuwen
Zhong, Bo
Tien, Po
Li, Shu
An, Tai
AuthorAffiliation 2 The College of Basic Medical Science, Shaanxi University of Chinese Medicine, Xi’an, China
The University of Chicago, UNITED STATES
1 The College of Life Sciences, State Key Laboratory of Virology, Modern Virology Research Center, Wuhan University, Wuhan, China
AuthorAffiliation_xml – name: 2 The College of Basic Medical Science, Shaanxi University of Chinese Medicine, Xi’an, China
– name: 1 The College of Life Sciences, State Key Laboratory of Virology, Modern Virology Research Center, Wuhan University, Wuhan, China
– name: The University of Chicago, UNITED STATES
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ContentType Journal Article
Copyright COPYRIGHT 2015 Public Library of Science
2015 An et al 2015 An et al
2015 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: An T, Li S, Pan W, Tien P, Zhong B, Shu H-B, et al. (2015) DYRK2 Negatively Regulates Type I Interferon Induction by Promoting TBK1 Degradation via Ser527 Phosphorylation. PLoS Pathog 11(9): e1005179. doi:10.1371/journal.ppat.1005179
Copyright_xml – notice: COPYRIGHT 2015 Public Library of Science
– notice: 2015 An et al 2015 An et al
– notice: 2015 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: An T, Li S, Pan W, Tien P, Zhong B, Shu H-B, et al. (2015) DYRK2 Negatively Regulates Type I Interferon Induction by Promoting TBK1 Degradation via Ser527 Phosphorylation. PLoS Pathog 11(9): e1005179. doi:10.1371/journal.ppat.1005179
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Conceived and designed the experiments: TA SW. Performed the experiments: TA SL WP. Analyzed the data: TA PT BZ HBS SW. Contributed reagents/materials/analysis tools: BZ HBS SW. Wrote the paper: TA BZ SW. Obtained permission for use of cell line: HBS.
The authors have declared that no competing interests exist.
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Snippet Viral infection activates the transcription factors NF-κB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral...
  Viral infection activates the transcription factors NF-KB and IRF3, which contribute to the induction of type I interferons (IFNs) and cellular antiviral...
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StartPage e1005179
SubjectTerms Animals
Cytokines
Deoxyribonucleic acid
DNA
Dyrk Kinases
Enzyme-Linked Immunosorbent Assay
Health aspects
HEK293 Cells
HeLa Cells
Host-virus relationships
Humans
Immunoblotting
Immunoprecipitation
Infections
Interferon
Interferon Type I - biosynthesis
Interferon Type I - immunology
Kinases
Molecular Sequence Data
Observations
Phosphorylation
Plasmids
Polymerase Chain Reaction
Protein kinases
Protein Serine-Threonine Kinases - immunology
Protein Serine-Threonine Kinases - metabolism
Protein-Tyrosine Kinases - immunology
Protein-Tyrosine Kinases - metabolism
Regulation
RNA polymerase
RNA, Small Interfering
Serine - immunology
Serine - metabolism
Signal Transduction - immunology
Transcription factors
Transduction, Genetic
Viral infections
Virus Diseases - immunology
Virus Diseases - metabolism
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Title DYRK2 Negatively Regulates Type I Interferon Induction by Promoting TBK1 Degradation via Ser527 Phosphorylation
URI https://www.ncbi.nlm.nih.gov/pubmed/26407194
https://www.proquest.com/docview/1718077372
https://pubmed.ncbi.nlm.nih.gov/PMC4583546
https://doaj.org/article/1d28892acb59421dacbec751c724da81
http://dx.doi.org/10.1371/journal.ppat.1005179
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