Evidence map›Paper›PMID 27400376›Full record

ArticleSmall GTPases2016

Unsolved mysteries of Rag GTPase signaling in yeast.

Riko Hatakeyama, Claudio De Virgilio

Abstract read
In one paragraph

Article in Small GTPases, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–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

16 citing papers in PubMed.

  1. Article
  2. A tractable physical model for the yeast polarity predicts epistasis and fitness.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  3. Regulation of mTORC1 by the Rag GTPases.Biochemical Society transactions · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Frontiers in genetics · 2020
    Article
  10. Frontiers in microbiology · 2019
    Article
  11. The yeast HeLife · 2018
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
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

2 authors.

Riko Hatakeyamaa Department of Biology , University of Fribourg , Fribourg , Switzerland.
Claudio De Virgilioa Department of Biology , University of Fribourg , Fribourg , Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The target of rapamycin complex 1 (TORC1) plays a central role in controlling eukaryotic cell growth by fine-tuning anabolic and catabolic processes to the nutritional status of organisms and individual cells. Amino acids represent essential and primordial signals that modulate TORC1 activity through the conserved Rag family GTPases. These assemble, as part of larger lysosomal/vacuolar membrane-associated complexes, into heterodimeric sub-complexes, which typically comprise two paralogous Rag GTPases of opposite GTP-/GDP-loading status. The TORC1-stimulating/inhibiting states of these heterodimers are controlled by various guanine nucleotide exchange factor (GEF) and GTPase-activating protein (GAP) complexes, which are remarkably conserved in various eukaryotic model systems. Among the latter, the budding yeast Saccharomyces cerevisiae has been instrumental for the elucidation of basic aspects of Rag GTPase regulation and function. Here, we discuss the current state of the respective research, focusing on the major unsolved issues regarding the architecture, regulation, and function of the Rag GTPase containing complexes in yeast. Decoding these mysteries will undoubtedly further shape our understanding of the conserved and divergent principles of nutrient signaling in eukaryotes.

Indexed as

Amino AcidsGene Expression Regulation, FungalGTP PhosphohydrolasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsAmino AcidsGTP PhosphohydrolasesSaccharomyces cerevisiae ProteinsTORC1 protein complex, S cerevisiaeTranscription Factorsamino acid signalingEGO complex (EGOC)Lst4-Lst7Rag GTPasesSEACATSEACITTarget of Rapamycin Complex 1 (TORC1)yeast

Identifiers

PMID27400376
PMCPMC5129903

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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.