Evidence map›Paper›PMID 38636948›Full record

ArticleNucleic acids research2024

Caspase-mediated processing of TRBP regulates apoptosis during viral infection.

Keiko Shibata, Harune Moriizumi, Koji Onomoto, Yuka Kaneko, Takuya Miyakawa, Shuhei Zenno, Masaru Tanokura, Mitsutoshi Yoneyama, Tomoko Takahashi, Kumiko Ui-Tei

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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

10 authors at 5 institutions in 1 country.

Keiko ShibataDepartment of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.
Harune MoriizumiDepartment of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.
Koji OnomotoDivision of Molecular Immunology, Medical Mycology Research Center, Chiba University, Chiba 260-8673, Japan.
Yuka KanekoDepartment of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.
Takuya MiyakawaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.
Shuhei ZennoDepartment of Biotechnology, Faculty of Engineering, Maebashi Institute of Technology, Gunma 371-0816, Japan.
Masaru TanokuraDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.ORCID 0000-0001-5072-2480
Mitsutoshi YoneyamaDivision of Molecular Immunology, Medical Mycology Research Center, Chiba University, Chiba 260-8673, Japan.
Tomoko TakahashiDepartment of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.ORCID 0000-0002-5094-8882
Kumiko Ui-TeiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.ORCID 0000-0001-8695-9025
Saitama University · JPChiba University · JPThe University of Tokyo · JPKyoto University · JPMaebashi Institute of Technology · JP

Funding

Canon FoundationChiba University 14-14Hitachi Global FoundationMinistry of Education 21310123MSD Life Science FoundationNaito Science & Engineering FoundationSECOM Science and Technology FoundationTakeda Science Foundation
6 · The paper itself

Abstract

RNA silencing is a post-transcriptional gene-silencing mechanism mediated by microRNAs (miRNAs). However, the regulatory mechanism of RNA silencing during viral infection is unclear. TAR RNA-binding protein (TRBP) is an enhancer of RNA silencing that induces miRNA maturation by interacting with the ribonuclease Dicer. TRBP interacts with a virus sensor protein, laboratory of genetics and physiology 2 (LGP2), in the early stage of viral infection of human cells. Next, it induces apoptosis by inhibiting the maturation of miRNAs, thereby upregulating the expression of apoptosis regulatory genes. In this study, we show that TRBP undergoes a functional conversion in the late stage of viral infection. Viral infection resulted in the activation of caspases that proteolytically processed TRBP into two fragments. The N-terminal fragment did not interact with Dicer but interacted with type I interferon (IFN) signaling modulators, such as protein kinase R (PKR) and LGP2, and induced ER stress. The end results were irreversible apoptosis and suppression of IFN signaling. Our results demonstrate that the processing of TRBP enhances apoptosis, reducing IFN signaling during viral infection.

Indexed as

ApoptosisCaspasesRNA-Binding ProteinsCell LineeIF-2 KinaseEndoplasmic Reticulum StressHEK293 CellsHeLa CellsHumansInterferon Type IMicroRNAsRibonuclease IIISignal TransductionTrans-Activation Responsive RNA-Binding ProteinVirus DiseasesCaspasesEIF2AK2 protein, humaneIF-2 KinaseInterferon Type IMicroRNAsRibonuclease IIIRNA-Binding ProteinsTrans-Activation Responsive RNA-Binding Protein

Identifiers

PMID38636948
PMCPMC11109963
OpenAlexW4394962106

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

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.