Evidence map›Paper›PMID 30371886›Full record

ArticleNucleic acids research2019

TOE1 acts as a 3' exonuclease for telomerase RNA and regulates telomere maintenance.

Tingting Deng, Yan Huang, Kai Weng, Song Lin, Yujing Li, Guang Shi, Yali Chen, Junjiu Huang, Dan Liu, Wenbin Ma and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 60 citations in OpenAlex.

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  16. Sm complex assembly and 5' cap trimethylation promote selective processing of snRNAs by the 3' exonuclease TOE1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. c-Jun N-terminal kinase signaling in aging.Frontiers in aging neuroscience · 2024
    Review
  18. Functional Insight into hTRIR.Current molecular medicine · 2024
    Article
  19. Review
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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

11 authors at 3 institutions in 2 countries.

Tingting DengState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Yan HuangState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Kai WengGuangzhou Institute of Pediatrics, Guangzhou Women and Children's Medical Centre, Guangzhou 510623, China.
Song LinState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Yujing LiState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Guang ShiState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Yali ChenState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Junjiu HuangState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Dan LiuVerna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Wenbin MaState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Zhou SongyangState Key Laboratory of Oncology in South China, Cancer Center, Collaborative Innovation Center for Cancer Medicine, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Sun Yat-sen University · CNBaylor College of Medicine · USGuangzhou Women and Children Medical Center · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In human cells, telomeres are elongated by the telomerase complex that contains the reverse transcriptase hTERT and RNA template TERC/hTR. Poly(A)-specific ribonuclease (PARN) is known to trim hTR precursors by removing poly(A) tails. However, the precise mechanism of hTR 3' maturation remains largely unknown. Target of Egr1 (TOE1) is an Asp-Glu-Asp-Asp (DEDD) domain containing deadenylase that is mutated in the human disease Pontocerebella Hypoplasia Type 7 (PCH7) and implicated in snRNA and hTR processing. We have previously found TOE1 to localize specifically in Cajal bodies, where telomerase RNP complex assembly takes place. In this study, we showed that TOE1 could interact with hTR and the telomerase complex. TOE1-deficient cells accumulated hTR precursors, including oligoadenylated and 3'-extended forms, which was accompanied by impaired telomerase activity and shortened telomeres. Telomerase activity in TOE1-deficient cells could be rescued by wild-type TOE1 but not the catalytically inactive mutant. Our results suggest that hTR 3' end processing likely involves multiple exonucleases that work in parallel and/or sequentially, where TOE1 may function non-redundantly as a 3'-to-5' exonuclease in conjunction with PARN. Our study highlights a mechanistic link between TOE1 mutation, improper hTR processing and telomere dysfunction in diseases such as PCH7.

Indexed as

Cerebellar DiseasesExonucleasesExoribonucleasesHeLa CellsHumansMutationNuclear ProteinsRNATelomeraseTelomereTelomere HomeostasisExonucleasesExoribonucleasesNuclear ProteinsRNATelomerasetelomerase RNATERT protein, humanTOE1 protein, human

Identifiers

PMID30371886
PMCPMC6326811
OpenAlexW2898699401

What OpenQuestion holds

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LicenceCC BY
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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.