Evidence map›Paper›PMID 23149688›Full record

ArticleMolecular systems biology2012

Regulation of yeast central metabolism by enzyme phosphorylation.

Ana Paula Oliveira, Christina Ludwig, Paola Picotti, Maria Kogadeeva, Ruedi Aebersold, Uwe Sauer

Abstract read
In one paragraph

Article in Molecular systems biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

86 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Impact of CRISPRi-Mediated Titration ofACS synthetic biology · 2025
    Article
  7. Article
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  11. The regulatory landscape of the yeast phosphoproteome.Nature structural & molecular biology · 2023
    Article
  12. Article
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  14. Article
  15. Article
  16. Review
  17. Article
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  20. Review

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

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.

Ana Paula OliveiraDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Christina Ludwig
Paola Picotti
Maria Kogadeeva
Ruedi Aebersold
Uwe Sauer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As a frequent post-translational modification, protein phosphorylation regulates many cellular processes. Although several hundred phosphorylation sites have been mapped to metabolic enzymes in Saccharomyces cerevisiae, functionality was demonstrated for few of them. Here, we describe a novel approach to identify in vivo functionality of enzyme phosphorylation by combining flux analysis with proteomics and phosphoproteomics. Focusing on the network of 204 enzymes that constitute the yeast central carbon and amino-acid metabolism, we combined protein and phosphoprotein levels to identify 35 enzymes that change their degree of phosphorylation during growth under five conditions. Correlations between previously determined intracellular fluxes and phosphoprotein abundances provided first functional evidence for five novel phosphoregulated enzymes in this network, adding to nine known phosphoenzymes. For the pyruvate dehydrogenase complex E1 α subunit Pda1 and the newly identified phosphoregulated glycerol-3-phosphate dehydrogenase Gpd1 and phosphofructose-1-kinase complex β subunit Pfk2, we then validated functionality of specific phosphosites through absolute peptide quantification by targeted mass spectrometry, metabolomics and physiological flux analysis in mutants with genetically removed phosphosites. These results demonstrate the role of phosphorylation in controlling the metabolic flux realised by these three enzymes.

Indexed as

Amino AcidsAmino Acid SequenceBiocatalysisCarbonMetabolic Networks and PathwaysMolecular Sequence DataPhosphopeptidesPhosphoproteinsPhosphorylationProteomeReproducibility of ResultsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmino AcidsCarbonPhosphopeptidesPhosphoproteinsProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID23149688
PMCPMC3531909

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.