Evidence map›Paper›PMID 40593584›Full record

ArticleNature communications2025

NONO, SFPQ, and PSPC1 promote telomerase recruitment to the telomere.

Alexander P Sobinoff, Jadon K Wells, Maurice Chow, Christopher B Nelson, Xinyi Wu, Scott B Cohen, Yu Heng Lau, Tracy M Bryan, Archa Fox, Hilda A Pickett

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Article
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.

Alexander P SobinoffTelomere Length Regulation Unit, Children's Medical Research Institute, Faculty of Medicine and Health, The University of Sydney, Westmead, NSW, Australia.ORCID http://orcid.org/0000-0001-6679-5211
Jadon K WellsTelomere Length Regulation Unit, Children's Medical Research Institute, Faculty of Medicine and Health, The University of Sydney, Westmead, NSW, Australia.ORCID http://orcid.org/0009-0007-4809-827X
Maurice ChowTelomere Length Regulation Unit, Children's Medical Research Institute, Faculty of Medicine and Health, The University of Sydney, Westmead, NSW, Australia.
Christopher B NelsonTelomere Length Regulation Unit, Children's Medical Research Institute, Faculty of Medicine and Health, The University of Sydney, Westmead, NSW, Australia.
Xinyi WuSchool of Chemistry, The University of Sydney, Camperdown, NSW, Australia.
Scott B CohenCell Biology Unit, Children's Medical Research Institute, Faculty of Medicine and Health, The University of Sydney, Westmead, NSW, Australia.
Yu Heng LauSchool of Chemistry, The University of Sydney, Camperdown, NSW, Australia.ORCID http://orcid.org/0000-0001-6560-8410
Tracy M BryanCell Biology Unit, Children's Medical Research Institute, Faculty of Medicine and Health, The University of Sydney, Westmead, NSW, Australia.ORCID http://orcid.org/0000-0002-7990-5501
Archa FoxSchool of Human Sciences, The University of Western Australia, Perth, WA, Australia.ORCID http://orcid.org/0000-0003-1962-270X
Hilda A PickettTelomere Length Regulation Unit, Children's Medical Research Institute, Faculty of Medicine and Health, The University of Sydney, Westmead, NSW, Australia. hpickett@cmri.org.au.ORCID http://orcid.org/0000-0002-9840-4841

Funding

Cancer Institute NSW (Cancer Institute New South Wales) ECF171269Department of Health | National Health and Medical Research Council (NHMRC) 2003250
6 · The paper itself

Abstract

Telomerase is a ribonucleoprotein enzyme that maintains telomeric repeats on chromosome ends in continuously dividing cells. Telomere maintenance via telomerase is dependent on the correct assembly of the enzyme complex, complex stabilization by associated cofactors, and effective recruitment to the telomere. Here, we show that telomerase is regulated in each of these processes by the Drosophila behaviour/human splicing (DBHS) family of RNA/DNA binding proteins (NONO, SFPQ and PSPC1). The DBHS proteins associate with catalytically active telomerase through the hTR RNA template component. Cells lacking the DBHS proteins display telomerase retention in nuclear Cajal bodies and impaired telomerase recruitment to the telomere, with NONO and PSPC1 depletion culminating in progressive telomere shortening in several cell lines, with the exception of long-term NONO depletion in 293 and 293T. Our results reveal the DBHS protein family as components of the telomerase trafficking machinery integral to telomere maintenance.

Indexed as

DNA-Binding ProteinsDrosophila ProteinsNuclear ProteinsRNA-Binding ProteinsTelomeraseTelomereAnimalsCoiled BodiesHEK293 CellsHumansMolecular ChaperonesPTB-Associated Splicing FactorRNADNA-Binding ProteinsDrosophila ProteinsMolecular ChaperonesNuclear ProteinsPTB-Associated Splicing FactorRNARNA-Binding ProteinsTelomeraseWRAP53 protein, human

Identifiers

PMID40593584
PMCPMC12218506

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.