Evidence map›Paper›PMID 27580159›Full record

ReviewSmall GTPases2016

Rags to riches: Amino acid sensing by the Rag GTPases in health and disease.

Owen A Brady, Heba I Diab, Rosa Puertollano

Open access · bronzeAbstract readReview
In one paragraph

Review in Small GTPases, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Regulation of mTORC1 by the Rag GTPases.Biochemical Society transactions · 2023
    Review
  5. Role of Diet in Stem and Cancer Stem Cells.International journal of molecular sciences · 2022
    Review
  6. mTOR Activity and Autophagy in Senescent Cells, a Complex Partnership.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Amino Acids in Autophagy: Regulation and Function.Advances in experimental medicine and biology · 2021
    Article
  9. Article
  10. 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 2 institutions in 1 country.

Owen A Bradya Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda , MD , USA.
Heba I Diaba Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda , MD , USA.
Rosa Puertollanoa Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda , MD , USA.
National Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

Lysosome biogenesis and homeostasisZIAHL006151 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI PUERTOLLANO, ROSA · 2012 to 2025
$15.0M
6 · The paper itself

Abstract

The Rags represent a unique family of evolutionarily conserved, heterodimeric, lysosome-localized small GTPases that play an indispensible role in regulating cellular metabolism in response to various amino acid signaling mechanisms. Rapid progress in the field has begun to unveil a picture in which Rags act as central players in translating information regarding cellular amino acid levels by modulating their nucleotide binding status through an ensemble of support proteins localized in and around the lysosomes. By cooperating with other signaling pathways that converge on the lysosomes, Rags promote anabolic processes through positively affecting mTORC1 signaling in the presence of abundant amino acids. Conversely, Rag inactivation plays an indispensible role in switching cellular metabolism into a catabolic paradigm by promoting the activity of the master lysosomal/autophagic transcription factors TFEB and TFE3. Precise control of Rag signaling is necessary for cells to adapt to constantly changing cellular demands and emerging evidence has highlighted their importance in a wide variety of developmental and pathological conditions.

Indexed as

Amino AcidsBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsBinding SitesDNA-Binding ProteinsHumansLysosomesMechanistic Target of Rapamycin Complex 1Monomeric GTP-Binding ProteinsMultiprotein ComplexesSignal TransductionTOR Serine-Threonine KinasesAmino AcidsBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsDNA-Binding ProteinsMechanistic Target of Rapamycin Complex 1Monomeric GTP-Binding ProteinsMultiprotein ComplexesTOR Serine-Threonine KinasesautophagylysosomesmTORRagsTFE3TFEB

Identifiers

PMID27580159
PMCPMC5129890
OpenAlexW2516435313

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.