Evidence map›Paper›PMID 36059259›Full record

ArticleThe EMBO journal2022

Rap1 prevents fusions between long telomeres in fission yeast.

Lili Pan, Duncan Tormey, Nadine Bobon, Peter Baumann

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2022. 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
0.4field-weighted citation impact, top 27% 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, 2 citations in OpenAlex.

  1. Article
  2. 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

4 authors at 2 institutions in 2 countries.

Lili PanDepartment of Biology, Johannes Gutenberg University, Mainz, Germany.ORCID 0000-0002-6110-1839
Duncan TormeyStowers Institute for Medical Research, Kansas City, MO, USA.ORCID 0000-0002-0963-3424
Nadine BobonDepartment of Biology, Johannes Gutenberg University, Mainz, Germany.
Peter BaumannDepartment of Biology, Johannes Gutenberg University, Mainz, Germany.ORCID 0000-0003-4892-1485
Johannes Gutenberg University Mainz · DEStowers Institute for Medical Research · US

Funding

Howard Hughes Medical Institute (HHMI)
6 · The paper itself

Abstract

The conserved Rap1 protein is part of the shelterin complex that plays critical roles in chromosome end protection and telomere length regulation. Previous studies have addressed how fission yeast Rap1 contributes to telomere length maintenance, but the mechanism by which the protein inhibits end fusions has remained elusive. Here, we use a mutagenesis screen in combination with high-throughput sequencing to identify several amino acid positions in Rap1 that have key roles in end protection. Interestingly, mutations at these sites render cells susceptible to genome instability in a conditional manner, whereby longer telomeres are prone to undergoing end fusions, while telomeres within the normal length range are sufficiently protected. The protection of long telomeres is in part dependent on their nuclear envelope attachment mediated by the Rap1-Bqt4 interaction. Our data demonstrate that long telomeres represent a challenge for the maintenance of genome integrity, thereby providing an explanation for species-specific upper limits on telomere length.

Indexed as

SchizosaccharomycesSchizosaccharomyces pombe ProteinsAmino AcidsShelterin ComplexTelomereTelomere-Binding ProteinsTelomere HomeostasisAmino AcidsRap1 protein, S pombeSchizosaccharomyces pombe ProteinsShelterin ComplexTelomere-Binding Proteinsend fusionsfission yeastgenome instabilityRap1telomere length

Identifiers

PMID36059259
PMCPMC9574727
OpenAlexW4294578512

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.