Evidence map›Paper›PMID 24788966›Full record

ArticlePloS one2014

Mitochondria-nucleus shuttling FK506-binding protein 51 interacts with TRAF proteins and facilitates the RIG-I-like receptor-mediated expression of type I IFN.

Taishin Akiyama, Takuma Shiraishi, Junwen Qin, Hiroyasu Konno, Nobuko Akiyama, Miho Shinzawa, Maki Miyauchi, Nobukazu Takizawa, Hiromi Yanai, Hiroyuki Ohashi and 5 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Knocking out Fkbp51 decreases CClCell & bioscience · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. The Many Faces of FKBP51.Biomolecules · 2019
    Review
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 3 institutions in 3 countries.

Taishin AkiyamaDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Takuma ShiraishiDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Junwen QinDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan; Department of Developmental and Regenerative Biology, Key Laboratory for Regenerative Medicine, Ministry of Education and International Base of Collaboration for Science and Technology, the Ministry of Science and Technology and Guangdong Province, Jinan University, Guangzhou, China.
Hiroyasu KonnoDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Nobuko AkiyamaDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Miho ShinzawaDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Maki MiyauchiDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Nobukazu TakizawaDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Hiromi YanaiDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Hiroyuki OhashiDivision of Interactome Medical Sciences, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Etsuko Miyamoto-SatoDivision of Interactome Medical Sciences, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
Hiroshi YanagawaDepartment of Biosciences and Informatics, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Weidong YongPediatrics, Biochemistry and Molecular Biology, Medical and Molecular Genetics, Pharmacology and Toxicology, Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, Indiana, United States of America.
Weinian ShouPediatrics, Biochemistry and Molecular Biology, Medical and Molecular Genetics, Pharmacology and Toxicology, Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, Indiana, United States of America.
Jun-Ichiro InoueDivision of Cellular and Molecular Biology, Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo, Japan.
The University of Tokyo · JPIndiana University School of MedicineKeio University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Virus-derived double-stranded RNAs (dsRNAs) are sensed in the cytosol by retinoic acid-inducible gene (RIG)-I-like receptors (RLRs). These induce the expression of type I IFN and proinflammatory cytokines through signaling pathways mediated by the mitochondrial antiviral signaling (MAVS) protein. TNF receptor-associated factor (TRAF) family proteins are reported to facilitate the RLR-dependent expression of type I IFN by interacting with MAVS. However, the precise regulatory mechanisms remain unclear. Here, we show the role of FK506-binding protein 51 (FKBP51) in regulating the dsRNA-dependent expression of type I IFN. The binding of FKBP51 to TRAF6 was first identified by "in vitro virus" selection and was subsequently confirmed with a coimmunoprecipitation assay in HEK293T cells. The TRAF-C domain of TRAF6 is required for its interaction, although FKBP51 does not contain the consensus motif for interaction with the TRAF-C domain. Besides TRAF6, we found that FKBP51 also interacts with TRAF3. The depletion of FKBP51 reduced the expression of type I IFN induced by dsRNA transfection or Newcastle disease virus infection in murine fibroblasts. Consistent with this, the FKBP51 depletion attenuated dsRNA-mediated phosphorylations of IRF3 and JNK and nuclear translocation of RelA. Interestingly, dsRNA stimulation promoted the accumulation of FKBP51 in the mitochondria. Moreover, the overexpression of FKBP51 inhibited RLR-dependent transcriptional activation, suggesting a scaffolding function for FKBP51 in the MAVS-mediated signaling pathway. Overall, we have demonstrated that FKBP51 interacts with TRAF proteins and facilitates the expression of type I IFN induced by cytosolic dsRNA. These findings suggest a novel role for FKBP51 in the innate immune response to viral infection.

Indexed as

Gene Expression RegulationAnimalsCell LineCell NucleusHumansImmunity, InnateInterferon Type IMiceMitochondriaNewcastle disease virusProtein BindingProtein Interaction MappingProtein Interaction MapsProtein TransportRNA, Double-StrandedSignal TransductionInterferon Type IRNA, Double-StrandedTacrolimus Binding Protein 5Tacrolimus Binding ProteinsTNF Receptor-Associated Factor 3TNF Receptor-Associated Factor 6Tumor Necrosis Factor Receptor-Associated Peptides and Proteins

Identifiers

PMID24788966
PMCPMC4006813
OpenAlexW2143548007

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.