Evidence map›Paper›PMID 31379141›Full record

ReviewJournal of Zhejiang University. Science. B

Sensors for the mTORC1 pathway regulated by amino acids.

Xiu-Zhi Li, Xiang-Hua Yan

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of Zhejiang University. Science. B. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Animal amino acid sensor - A review.Animal bioscience · 2025
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. AmSphere · 2024
    Article
  11. Article
  12. mTOR Complex 1 Content and Regulation Is Adapted to Animal Longevity.International journal of molecular sciences · 2022
    Review
  13. A dynamically evolving war between autophagy and pathogenic microorganisms.Journal of Zhejiang University. Science. B · 2022
    Article
  14. Dairy consumption and hepatocellular carcinoma risk.Annals of translational medicine · 2021
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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 at 1 institution in 1 country.

Xiu-Zhi LiState Key Laboratory of Agricultural Microbiology, College of Animal Sciences and Technology, Huazhong Agricultural University, Wuhan 430070, China.
Xiang-Hua YanState Key Laboratory of Agricultural Microbiology, College of Animal Sciences and Technology, Huazhong Agricultural University, Wuhan 430070, China.
Huazhong Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to various environmental inputs, especially amino acids. In fact, the activity of mTORC1 is highly sensitive to changes in amino acid levels. Over past decades, a variety of proteins have been identified as participating in the mTORC1 pathway regulated by amino acids. Classically, the Rag guanosine triphosphatases (GTPases), which reside on the lysosome, transmit amino acid availability to the mTORC1 pathway and recruit mTORC1 to the lysosome upon amino acid sufficiency. Recently, several sensors of leucine, arginine, and S-adenosylmethionine for the amino acid-stimulated mTORC1 pathway have been coming to light. Characterization of these sensors is requisite for understanding how cells adjust amino acid sensing pathways to their different needs. In this review, we summarize recent advances in amino acid sensing mechanisms that regulate mTORC1 activity and highlight these identified sensors that accurately transmit specific amino acid signals to the mTORC1 pathway.

Indexed as

Amino AcidsAnimalsArginineCell MembraneGene Expression RegulationGolgi ApparatusGTP PhosphohydrolasesHumansLeucineLysosomesMechanistic Target of Rapamycin Complex 1MethionineS-AdenosylmethionineSignal TransductionTOR Serine-Threonine KinasesAmino AcidsArginineGTP PhosphohydrolasesLeucineMechanistic Target of Rapamycin Complex 1MethionineS-AdenosylmethionineTOR Serine-Threonine KinasesMechanistic target of rapamycin complex 1 (mTORC1); Amino acid; Sensor; Lysosome; Rag GTPases

Identifiers

PMID31379141
PMCPMC6700350
OpenAlexW2964847205

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.