Evidence map›Paper›PMID 20702584›Full record

ArticleMolecular biology of the cell2010

The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates.

Alexandre Soulard, Alessio Cremonesi, Suzette Moes, Frédéric Schütz, Paul Jenö, Michael N Hall

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 168 papers.

0numbers the graph read from it
0cells of the map it votes in
168citing papers in PubMed
6.9field-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

168 citing papers in PubMed, 270 citations in OpenAlex.

  1. Article
  2. Regulation of Translation by PKA Signaling Pathway.International journal of molecular sciences · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Integrative Phosphoproteomic and Proteomic Analysis ofJournal of proteome research · 2025
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Review
  17. Article
  18. Article
  19. Review
  20. Article

108 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 at 1 institution in 1 country.

Alexandre SoulardBiozentrum, University of Basel, CH-4056 Basel, Switzerland.
Alessio Cremonesi
Suzette Moes
Frédéric Schütz
Paul Jenö
Michael N Hall
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulation of cell growth requires extensive coordination of several processes including transcription, ribosome biogenesis, translation, nutrient metabolism, and autophagy. In yeast, the protein kinases Target of Rapamycin (TOR) and protein kinase A (PKA) regulate these processes and are thereby the main activators of cell growth in response to nutrients. How TOR, PKA, and their corresponding signaling pathways are coordinated to control the same cellular processes is not understood. Quantitative analysis of the rapamycin-sensitive phosphoproteome combined with targeted analysis of PKA substrates suggests that TOR complex 1 (TORC1) activates PKA but only toward a subset of substrates. Furthermore, we show that TORC1 signaling impinges on BCY1, the negative regulatory subunit of PKA. Inhibition of TORC1 with rapamycin leads to BCY1 phosphorylation on several sites including T129. Phosphorylation of BCY1 T129 results in BCY1 activation and inhibition of PKA. TORC1 inhibits BCY1 T129 phosphorylation by phosphorylating and activating the S6K homolog SCH9 that in turn inhibits the MAP kinase MPK1. MPK1 phosphorylates BCY1 T129 directly. Thus, TORC1 activates PKA toward some substrates by preventing MPK1-mediated activation of BCY1.

Indexed as

Amino Acid SequenceCyclic AMP-Dependent Protein KinasesEnzyme ActivationIsotope LabelingMolecular Sequence DataPhosphopeptidesPhosphoproteinsPhosphorylationPhosphothreonineProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSirolimusSubstrate SpecificityTOR Serine-Threonine KinasesTranscription FactorsCyclic AMP-Dependent Protein KinasesPhosphopeptidesPhosphoproteinsPhosphothreonineProteomeSaccharomyces cerevisiae ProteinsSirolimusTOR Serine-Threonine KinasesTranscription Factors

Identifiers

PMID20702584
PMCPMC2947482
OpenAlexW2125025556

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.