Evidence map›Paper›PMID 32198460›Full record

ArticleScientific reports2020

Structural analysis of TIFA: Insight into TIFA-dependent signal transduction in innate immunity.

Teruya Nakamura, Chie Hashikawa, Kohtaro Okabe, Yuya Yokote, Mami Chirifu, Sachiko Toma-Fukai, Narushi Nakamura, Mihoko Matsuo, Miho Kamikariya, Yoshinari Okamoto and 7 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 48% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. TIFAB regulates the TIFA-TRAF6 signaling pathway involved in innate immunity by forming a heterodimer complex with TIFA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. 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

17 authors at 5 institutions in 1 country.

Teruya NakamuraGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan. tnaka@gpo.kumamoto-u.ac.jp.
Chie HashikawaGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan.
Kohtaro OkabeSchool of Pharmacy, Kumamoto University, Kumamoto, Japan.
Yuya YokoteSchool of Pharmacy, Kumamoto University, Kumamoto, Japan.
Mami ChirifuGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan.
Sachiko Toma-FukaiGraduate School of Science and Technology, Nara Institute of Science and Technology, Ikoma, Japan.
Narushi NakamuraSchool of Pharmacy, Kumamoto University, Kumamoto, Japan.
Mihoko MatsuoPriority Organization for Innovation and Excellence, Kumamoto University, Kumamoto, Japan.
Miho KamikariyaSchool of Pharmacy, Kumamoto University, Kumamoto, Japan.
Yoshinari OkamotoGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan.
Jin GohdaResearch Center for Asian Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Taishin AkiyamaLaboratory for Immune Homeostasis, RIKEN Center for Integrative Medical Sciences, Yokohama, Japan.
Kentaro SembaDepartment of Life Science and Medical Bioscience, Waseda University, Tokyo, Japan.
Shinji IkemizuGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan.
Masami OtsukaGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan.
Jun-Ichiro InoueResearch Center for Asian Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Yuriko YamagataGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan.
Kumamoto University · JPThe University of Tokyo · JPNara Institute of Science and Technology · JPRIKEN Center for Integrative Medical Sciences · JPWaseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRAF-interacting protein with a forkhead-associated (FHA) domain (TIFA), originally identified as an adaptor protein of TRAF6, has recently been shown to be involved in innate immunity, induced by a pathogen-associated molecular pattern (PAMP). ADP-β-D-manno-heptose, a newly identified PAMP, binds to alpha-kinase 1 (ALPK1) and activates its kinase activity to phosphorylate TIFA. Phosphorylation triggers TIFA oligomerisation and formation of a subsequent TIFA-TRAF6 oligomeric complex for ubiquitination of TRAF6, eventually leading to NF-κB activation. However, the structural basis of TIFA-dependent TRAF6 signalling, especially oligomer formation of the TIFA-TRAF6 complex remains unknown. In the present study, we determined the crystal structures of mouse TIFA and two TIFA mutants-Thr9 mutated to either Asp or Glu to mimic the phosphorylation state-to obtain the structural information for oligomer formation of the TIFA-TRAF6 complex. Crystal structures show the dimer formation of mouse TIFA to be similar to that of human TIFA, which was previously reported. This dimeric structure is consistent with the solution structure obtained from small angle X-ray scattering analysis. In addition to the structural analysis, we examined the molecular assembly of TIFA and the TIFA-TRAF6 complex by size-exclusion chromatography, and suggested a model for the TIFA-TRAF6 signalling complex.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsHumansImmunity, InnateIntracellular Signaling Peptides and ProteinsMiceNF-kappa BPathogen-Associated Molecular Pattern MoleculesPhosphorylationProtein KinasesSignal TransductionTNF Receptor-Associated Factor 6Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsUbiquitinationAdaptor Proteins, Signal TransducingALPK1 protein, humanIntracellular Signaling Peptides and ProteinsNF-kappa BPathogen-Associated Molecular Pattern MoleculesProtein KinasesTifab protein, humanTNF Receptor-Associated Factor 6Tumor Necrosis Factor Receptor-Associated Peptides and Proteins

Identifiers

PMID32198460
PMCPMC7083832
OpenAlexW3012269765

What OpenQuestion holds

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Registered trials

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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.