Evidence map›Paper›PMID 26551880›Full record

ArticleNature immunology2016

The cytotoxic T cell proteome and its shaping by the kinase mTOR.

Jens L Hukelmann, Karen E Anderson, Linda V Sinclair, Katarzyna M Grzes, Alejandro Brenes Murillo, Phillip T Hawkins, Len R Stephens, Angus I Lamond, Doreen A Cantrell

Open access · greenAbstract read
In one paragraph

Article in Nature immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 255 citations in OpenAlex.

  1. Article
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  7. Tissue-distinct Features of Follicular Cytotoxic CD8bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
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  11. Article
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  19. The NAE1-mediated neddylation operates as an essential post-translational modification checkpoint for effector CD8Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Review

87 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Jens L HukelmannDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dow Street, Dundee, UK.
Karen E AndersonInositide Laboratory, Babraham Institute, Babraham Research Campus, Cambridge, UK.
Linda V SinclairDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dow Street, Dundee, UK.
Katarzyna M GrzesDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dow Street, Dundee, UK.
Alejandro Brenes MurilloCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, UK.
Phillip T HawkinsInositide Laboratory, Babraham Institute, Babraham Research Campus, Cambridge, UK.
Len R StephensInositide Laboratory, Babraham Institute, Babraham Research Campus, Cambridge, UK.
Angus I LamondCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, UK.
Doreen A CantrellDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dow Street, Dundee, UK.
University of Dundee · GBBabraham Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/B/000C0413Biotechnology and Biological Sciences Research Council BBS/E/B/000C0415Wellcome Trust 065975/Z/01/AWellcome Trust 073980Wellcome Trust 073980/Z/03/ZWellcome Trust 093713Wellcome Trust 093713/Z/10/AWellcome Trust 097418Wellcome Trust 097418/Z/11/ZWellcome Trust 105024Wellcome Trust 105024/Z/14/Z
6 · The paper itself

Abstract

We used high-resolution mass spectrometry to map the cytotoxic T lymphocyte (CTL) proteome and the effect of the metabolic checkpoint kinase mTORC1 on CTLs. The CTL proteome was dominated by metabolic regulators and granzymes, and mTORC1 selectively repressed and promoted expression of a subset of CTL proteins (~10%). These included key CTL effector molecules, signaling proteins and a subset of metabolic enzymes. Proteomic data highlighted the potential for negative control of the production of phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3) by mTORC1 in CTLs. mTORC1 repressed PtdIns(3,4,5)P3 production and determined the requirement for mTORC2 in activation of the kinase Akt. Our unbiased proteomic analysis thus provides comprehensive understanding of CTL identity and the control of CTL function by mTORC1.

Indexed as

AnimalsCells, CulturedChromatographyEnzyme-Linked Immunosorbent AssayFemaleImmunoblottingMaleMass SpectrometryMechanistic Target of Rapamycin Complex 1MiceMultiprotein ComplexesOligonucleotide Array Sequence AnalysisProteomeT-Lymphocytes, CytotoxicTOR Serine-Threonine KinasesMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProteomeTOR Serine-Threonine Kinases

Identifiers

PMID26551880
PMCPMC4685757
OpenAlexW2191096966

What OpenQuestion holds

Textmetadata
LicenceTDM
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.