Evidence map›Paper›PMID 27841257›Full record

ArticleNature communications2016

Glucose-regulated and drug-perturbed phosphoproteome reveals molecular mechanisms controlling insulin secretion.

Francesca Sacco, Sean J Humphrey, Jürgen Cox, Marcel Mischnik, Anke Schulte, Thomas Klabunde, Matthias Schäfer, Matthias Mann

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

52 citing papers in PubMed, 116 citations in OpenAlex.

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  12. Isoform-specific C-terminal phosphorylation drives autoinhibition of Casein kinase 1.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  14. Mechanisms of spinophilin-dependent pancreas dysregulation in obesity.American journal of physiology. Endocrinology and metabolism · 2024
    Article
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  17. Review
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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

8 authors at 2 institutions in 2 countries.

Francesca SaccoDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.ORCID 0000-0001-5586-9529
Sean J HumphreyDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Jürgen CoxDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Marcel MischnikSanofi Aventis Deutschland GmbH, R&D, LGCR, SDI, Bioinformatics, Frankfurt 65926, Germany.
Anke SchulteSanofi Aventis Deutschland GmbH, Global Diabetes Division, R&TM, Islet Biology, Frankfurt 65926, Germany.
Thomas KlabundeSanofi Aventis Deutschland GmbH, R&D, LGCR, SDI, Bioinformatics, Frankfurt 65926, Germany.
Matthias SchäferSanofi Aventis Deutschland GmbH, Global Diabetes Division, R&TM, Islet Biology, Frankfurt 65926, Germany.
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Max Planck Institute of Biochemistry · DESanofi (France) · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin-secreting beta cells play an essential role in maintaining physiological blood glucose levels, and their dysfunction leads to the development of diabetes. To elucidate the signalling events regulating insulin secretion, we applied a recently developed phosphoproteomics workflow. We quantified the time-resolved phosphoproteome of murine pancreatic cells following their exposure to glucose and in combination with small molecule compounds that promote insulin secretion. The quantitative phosphoproteome of 30,000 sites clustered into three main groups in concordance with the modulation of the three key kinases: PKA, PKC and CK2A. A high-resolution time course revealed key novel regulatory sites, revealing the importance of methyltransferase DNMT3A phosphorylation in the glucose response. Remarkably a significant proportion of these novel regulatory sites is significantly downregulated in diabetic islets. Control of insulin secretion is embedded in an unexpectedly broad and complex range of cellular functions, which are perturbed by drugs in multiple ways.

Indexed as

AnimalsCell Line, TumorCluster AnalysisDiabetes Mellitus, Type 1GlucoseInsulinInsulin-Secreting CellsInsulin SecretionIslets of LangerhansMice, Inbred C57BLMice, Inbred NODPhosphoproteinsPhosphorylationProteomeProteomicsSmall Molecule LibrariesGlucoseInsulinPhosphoproteinsProteomeSmall Molecule Libraries

Identifiers

PMID27841257
PMCPMC5114537
OpenAlexW2551863723

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.