Evidence map›Paper›PMID 21154118›Full record

ReviewCurrent opinion in investigational drugs (London, England : 2000)2010

Intracellular amino acid sensing and mTORC1-regulated growth: new ways to block an old target?

Deborah C I Goberdhan

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in investigational drugs (London, England : 2000), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. mTORC1 as the main gateway to autophagy.Essays in biochemistry · 2017
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Deborah C I GoberdhanDepartment of Physiology, Anatomy and Genetics, University of Oxford, South Parks Road, Oxford, UK. deborah.goberdhan@dpag.ox.ac.uk
University of Oxford · GB

Funding

Cancer Research UK A6181Cancer Research UK A9093Cancer Research UK C19591/A6181
6 · The paper itself

Abstract

Mammalian target of rapamycin (mTOR) complex 1 (mTORC1) is a multicomponent, nutrient-sensitive protein that is implicated in a wide range of major human diseases. mTORC1 responds to both growth factors and changes in local amino acid levels. Until recently, the intracellular amino acid-sensing mechanism that regulates mTORC1 had remained unexplored. However, studies in human cells in culture have demonstrated that in response to amino acid stimulation, mTOR (a conserved member of the PI3K superfamily) is shuttled to late endosomal and lysosomal compartments, where it binds the Ragulator-Rag complex and is assembled into active mTORC1. Members of the proton-assisted amino acid transporter (PAT/SLC36) family have been identified as critical components of the amino acid-sensing system that regulates mTORC1 present in endosomal and lysosomal membranes. These discoveries not only highlight several new potential drug targets that could impact selectively on mTORC1 activity in cancer cells, but also provide novel insights into the strategies used by such cells to outcompete their neighbors in growth factor- and nutrient-depleted conditions. In this review, recent mechanistic insights into how mTORC1 activity is controlled by amino acids and the potential for the selective targeting this regulatory input are discussed.

Indexed as

Amino AcidsAmino Acid Transport SystemsAnimalsCytoplasmDipteraHumansIntracellular MembranesLysosomesMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesNeoplasmsNutritional Physiological PhenomenaProtein BindingProteinsSignal TransductionSirolimusAmino AcidsAmino Acid Transport SystemsMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProteinsSirolimusTOR Serine-Threonine Kinases

Identifiers

PMID21154118
PMCPMC3044466
OpenAlexW78262552

What OpenQuestion holds

Textmetadata
LicenceTDM
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.