Evidence map›Paper›PMID 11416207›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Carbon- and nitrogen-quality signaling to translation are mediated by distinct GATA-type transcription factors.

F G Kuruvilla, A F Shamji, S L Schreiber

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-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

35 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Staying alive: metabolic adaptations to quiescence.Cell cycle (Georgetown, Tex.) · 2012
    Review
  11. Article
  12. Regulation of entry into gametogenesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011
    Review
  13. Article
  14. Review
  15. Review
  16. Rapamycin inhibits yeast nucleotide excision repair independently of tor kinases.Toxicological sciences : an official journal of the Society of Toxicology · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

F G KuruvillaDepartment of Chemistry and Chemical Biology, Howard Hughes Medical Institute, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
A F Shamji
S L Schreiber
Harvard University · US

Funding

SYNTHESIS OF MATERIALS WITH PHYSIOLOGICAL PROPERTIESR01GM038627 · NIGMS · YALE UNIVERSITY · PI SCHREIBER, STUART L · 1987 to 2017
$10.5M
SYNTHESIS OF MATERIALS WITH PHYSIOLOGICAL PROPERTIESR37GM038627 · NIGMS · HARVARD UNIVERSITY · PI SCHREIBER, STUART L · 1992 to 2001
$1.1M
NIGMS NIH HHS GM-38627NIGMS NIH HHS R01 GM038627NIGMS NIH HHS R37 GM038627
6 · The paper itself

Abstract

The target of rapamycin (Tor) proteins sense nutrients and control transcription and translation relevant to cell growth. Treating cells with the immunosuppressant rapamycin leads to the intracellular formation of an Fpr1p-rapamycin-Tor ternary complex that in turn leads to translational down-regulation. A more rapid effect is a rich transcriptional response resembling that when cells are shifted from high- to low-quality carbon or nitrogen sources. This transcriptional response is partly mediated by the nutrient-sensitive transcription factors GLN3 and NIL1 (also named GAT1). Here, we show that these GATA-type transcription factors control transcriptional responses that mediate translation by several means. Four observations highlight upstream roles of GATA-type transcription factors in translation. In their absence, processes caused by rapamycin or poor nutrients are diminished: translation repression, eIF4G protein loss, transcriptional down-regulation of proteins involved in translation, and RNA polymerase I/III activity repression. The Tor proteins preferentially use Gln3p or Nil1p to down-regulate translation in response to low-quality nitrogen or carbon, respectively. Functional consideration of the genes regulated by Gln3p or Nil1p reveals the logic of this differential regulation. Besides integrating control of transcription and translation, these transcription factors constitute branches downstream of the multichannel Tor proteins that can be selectively modulated in response to distinct (carbon- and nitrogen-based) nutrient signals from the environment.

Indexed as

Protein BiosynthesisRepressor ProteinsSaccharomyces cerevisiae ProteinsTranscription, GeneticAmino AcidsBiological TransportCarbonCitric Acid CycleCulture MediaDNA-Binding ProteinsEnergy MetabolismFungal ProteinsGATA Transcription FactorsGene Expression Regulation, FungalModels, BiologicalNitrogenAmino AcidsCarbonCulture MediaDNA-Binding ProteinsFungal ProteinsGAT1 protein, S cerevisiaeGATA Transcription FactorsGLN3 protein, S cerevisiaeNitrogenRepressor ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID11416207
PMCPMC34660
OpenAlexW1988737528

What OpenQuestion holds

Textmetadata
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.