Evidence map›Paper›PMID 27080861›Full record

ArticleScientific reports2016

Integrative Phosphoproteomics Links IL-23R Signaling with Metabolic Adaptation in Lymphocytes.

Corinne Lochmatter, Roman Fischer, Philip D Charles, Zhanru Yu, Fiona Powrie, Benedikt M Kessler

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

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  16. PKM2-dependent metabolic reprogramming in CD4Journal of molecular medicine (Berlin, Germany) · 2018
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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

6 authors at 1 institution in 1 country.

Corinne LochmatterKennedy Institute, Nuffield Department of Orthopedics Research Medical Science, Roosevelt Drive, Oxford OX3 7LF, UK.
Roman FischerKennedy Institute, Nuffield Department of Orthopedics Research Medical Science, Roosevelt Drive, Oxford OX3 7LF, UK.
Philip D CharlesTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7FZ, UK.
Zhanru YuTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7FZ, UK.
Fiona PowrieKennedy Institute, Nuffield Department of Orthopedics Research Medical Science, Roosevelt Drive, Oxford OX3 7LF, UK.
Benedikt M KesslerTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7FZ, UK.
University of Oxford · GB

Funding

Medical Research Council MR/L022699/1Wellcome TrustWellcome Trust 097813/Z/11/Z
6 · The paper itself

Abstract

Interleukin (IL)-23 mediated signal transduction represents a major molecular mechanism underlying the pathology of inflammatory bowel disease, Crohn's disease and ulcerative colitis. In addition, emerging evidence supports the role of IL-23-driven Th17 cells in inflammation. Components of the IL-23 signaling pathway, such as IL-23R, JAK2 and STAT3, have been characterized, but elements unique to this network as compared to other interleukins have not been readily explored. In this study, we have undertaken an integrative phosphoproteomics approach to better characterise downstream signaling events. To this end, we performed and compared phosphopeptide and phosphoprotein enrichment methodologies after activation of T lymphocytes by IL-23. We demonstrate the complementary nature of the two phosphoenrichment approaches by maximizing the capture of phosphorylation events. A total of 8202 unique phosphopeptides, and 4317 unique proteins were identified, amongst which STAT3, PKM2, CDK6 and LASP-1 showed induction of specific phosphorylation not readily observed after IL-2 stimulation. Interestingly, quantitative analysis revealed predominant phosphorylation of pre-existing STAT3 nuclear subsets in addition to translocation of phosphorylated STAT3 within 30 min after IL-23 stimulation. After IL-23R activation, a small subset of PKM2 also translocates to the nucleus and may contribute to STAT3 phosphorylation, suggesting multiple cellular responses including metabolic adaptation.

Indexed as

Energy MetabolismProteomicsSignal TransductionActive Transport, Cell NucleusAdaptation, BiologicalCarrier ProteinsDatabases, ProteinGlycolysisHumansInterleukin-23LymphocytesMembrane ProteinsModels, BiologicalPhosphopeptidesPhosphoproteinsPhosphorylationCarrier ProteinsIL23R protein, humanInterleukin-23Membrane ProteinsPhosphopeptidesPhosphoproteinsReceptors, InterleukinSTAT3 Transcription FactorThyroid Hormone-Binding ProteinsThyroid Hormones

Identifiers

PMID27080861
PMCPMC4832251
OpenAlexW2341271443

What OpenQuestion holds

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Registered trials

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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.