Evidence map›Paper›PMID 24424027›Full record

ArticleJournal of cell science2014

Torin1-mediated TOR kinase inhibition reduces Wee1 levels and advances mitotic commitment in fission yeast and HeLa cells.

Jane Atkin, Lenka Halova, Jennifer Ferguson, James R Hitchin, Agata Lichawska-Cieslar, Allan M Jordan, Jonathon Pines, Claudia Wellbrock, Janni Petersen

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Cytoplasmic fluidization contributes to breaking spore dormancy in fission yeast.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

9 authors at 3 institutions in 1 country.

Jane AtkinFaculty of Life Sciences, University of Manchester, Michael Smith Building, Manchester M13 9PT, UK.
Lenka Halova
Jennifer Ferguson
James R Hitchin
Agata Lichawska-Cieslar
Allan M Jordan
Jonathon Pines
Claudia Wellbrock
Janni Petersen
University of Manchester · GBWellcome/Cancer Research UK Gurdon Institute · GBCancer Research UK Manchester Institute · GB

Funding

Cancer Research UK 11178Cancer Research UK 17098Cancer Research UK C10888/A11178Medical Research Council G1000818Wellcome Trust 092096
6 · The paper itself

Abstract

The target of rapamycin (TOR) kinase regulates cell growth and division. Rapamycin only inhibits a subset of TOR activities. Here we show that in contrast to the mild impact of rapamycin on cell division, blocking the catalytic site of TOR with the Torin1 inhibitor completely arrests growth without cell death in Schizosaccharomyces pombe. A mutation of the Tor2 glycine residue (G2040D) that lies adjacent to the key Torin-interacting tryptophan provides Torin1 resistance, confirming the specificity of Torin1 for TOR. Using this mutation, we show that Torin1 advanced mitotic onset before inducing growth arrest. In contrast to TOR inhibition with rapamycin, regulation by either Wee1 or Cdc25 was sufficient for this Torin1-induced advanced mitosis. Torin1 promoted a Polo and Cdr2 kinase-controlled drop in Wee1 levels. Experiments in human cell lines recapitulated these yeast observations: mammalian TOR (mTOR) was inhibited by Torin1, Wee1 levels declined and mitotic commitment was advanced in HeLa cells. Thus, the regulation of the mitotic inhibitor Wee1 by TOR signalling is a conserved mechanism that helps to couple cell cycle and growth controls.

Indexed as

Amino Acid SequenceCatalytic DomainCell Cycle ProteinsCell DeathDrug ResistanceG1 Phase Cell Cycle CheckpointsHeLa CellsHumansMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2MitosisMolecular Sequence DataMultiprotein ComplexesMutagenesis, Site-DirectedNaphthyridinesNuclear Proteins1-(4-(4-propionylpiperazin-1-yl)-3-(trifluoromethyl)phenyl)-9-(quinolin-3-yl)benzo(h)(1,6)naphthyridin-2(1H)-oneCell Cycle ProteinsMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Multiprotein ComplexesNaphthyridinesNuclear ProteinsPhosphatidylinositol 3-KinasesProtein-Tyrosine KinasesSchizosaccharomyces pombe Proteinstor2 protein, S pombeTOR Serine-Threonine KinasesWEE1 protein, humanwee1 protein, S pombeHeLaS. pombeTORTorin1Wee1

Identifiers

PMID24424027
PMCPMC3953821
OpenAlexW2135068342

What OpenQuestion 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 OpenQuestion graph.