Evidence map›Paper›PMID 30833605›Full record

ArticleScientific reports2019

Direct imaging of the recruitment and phosphorylation of S6K1 in the mTORC1 pathway in living cells.

Abdullah R Ahmed, Raymond J Owens, Christopher D Stubbs, Anthony W Parker, Richard Hitchman, Rahul B Yadav, Maud Dumoux, Chris Hawes, Stanley W Botchway

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

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  18. mTOR at the nexus of nutrition, growth, ageing and disease.Nature reviews. Molecular cell biology · 2020
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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.

Abdullah R AhmedCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0FA, UK.
Raymond J OwensProtein Production UK, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0FA, UK.
Christopher D StubbsCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0FA, UK.
Anthony W ParkerCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0FA, UK.ORCID 0000-0003-3094-9762
Richard HitchmanEvotec (UK) Ltd, 114 Innovation Drive, Milton Park, Abingdon, Oxfordshire, OX14 4RZ, UK.
Rahul B YadavEvotec (UK) Ltd, 114 Innovation Drive, Milton Park, Abingdon, Oxfordshire, OX14 4RZ, UK.
Maud DumouxProtein Production UK, Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0FA, UK.
Chris HawesOxford Brookes University, Headington Campus, Oxford, OX3 0BP, UK.
Stanley W BotchwayCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0FA, UK. stan.botchway@stfc.ac.uk.
Rutherford Appleton Laboratory · GBEvotec (United Kingdom) · GBOxford Brookes University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L016052/1Medical Research Council MR/K018779/1
6 · The paper itself

Abstract

Knowledge of protein signalling pathways in the working cell is seen as a primary route to identifying and developing targeted medicines. In recent years there has been a growing awareness of the importance of the mTOR pathway, making it an attractive target for therapeutic intervention in several diseases. Within this pathway we have focused on S6 kinase 1 (S6K1), the downstream phosphorylation substrate of mTORC1, and specifically identify its juxtaposition with mTORC1. When S6K1 is co-expressed with raptor we show that S6K1 is translocated from the nucleus to the cytoplasm. By developing a novel biosensor we demonstrate in real-time, that phosphorylation and de-phosphorylation of S6K1 occurs mainly in the cytoplasm of living cells. Furthermore, we show that the scaffold protein raptor, that typically recruits mTOR substrates, is not always involved in S6K1 phosphorylation. Overall, we demonstrate how FRET-FLIM imaging technology can be used to show localisation of S6K1 phosphorylation in living cells and hence a key site of action of inhibitors targeting mTOR phosphorylation.

Indexed as

HEK293 CellsHumansMechanistic Target of Rapamycin Complex 1MutationPhosphorylationProtein BindingRas Homolog Enriched in Brain ProteinRegulatory-Associated Protein of mTORRibosomal Protein S6 Kinases, 70-kDaSirolimusTOR Serine-Threonine KinasesMechanistic Target of Rapamycin Complex 1Ras Homolog Enriched in Brain ProteinRegulatory-Associated Protein of mTORribosomal protein S6 kinase, 70kD, polypeptide 1Ribosomal Protein S6 Kinases, 70-kDaSirolimusTOR Serine-Threonine Kinases

Identifiers

PMID30833605
PMCPMC6399282
OpenAlexW2919866161

What OpenQuestion holds

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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.