Evidence map›Paper›PMID 22749019›Full record

ReviewTrends in molecular medicine2012

Amino acids and mTORC1: from lysosomes to disease.

Alejo Efeyan, Roberto Zoncu, David M Sabatini

Open access · bronzeAbstract readReview
In one paragraph

Review in Trends in molecular medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 241 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
241citing papers in PubMed, 1 pooled it
19.3field-weighted citation impact, top 1% 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

241 citing papers in PubMed, 1 synthesis or guideline pooled it, 431 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Noncanonical PI(4,5)PScience advances · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. V-ATPase in cancer: mechanistic insights and therapeutic potentials.Cell communication and signaling : CCS · 2024
    Review
  14. Article
  15. Review
  16. GlobalNature metabolism · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

181 more citing papers are in PubMed but not listed here.

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.

Alejo EfeyanWhitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.
Roberto Zoncu
David M Sabatini
Broad Institute · US

Funding

Regulation of the mTOR Pathway By NutrientsR01CA103866 · NCI · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI WEISSMAN, JONATHAN S. · 2004 to 2021
$7.0M
Cell Growth Signaling in Cancer DevelopmentR01CA129105 · NCI · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI WEISSMAN, JONATHAN S. · 2008 to 2021
$5.9M
Novel Components of the mTORC1 and mTORC2 PathwaysR37AI047389 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI SABATINI, DAVID M. · 2010 to 2019
$4.8M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA103866NCI NIH HHS R01 CA129105NIAID NIH HHS R37 AI047389
6 · The paper itself

Abstract

The mechanistic target of rapamycin (mTOR) kinase controls growth and metabolism, and its deregulation underlies the pathogenesis of many diseases, including cancer, neurodegeneration, and diabetes. mTOR complex 1 (mTORC1) integrates signals arising from nutrients, energy, and growth factors, but how exactly these signals are propagated await to be fully understood. Recent findings have placed the lysosome, a key mediator of cellular catabolism, at the core of mTORC1 regulation by amino acids. A multiprotein complex that includes the Rag GTPases, Ragulator, and the v-ATPase forms an amino acid-sensing machinery on the lysosomal surface that affects the decision between cell growth and catabolism at multiple levels. The involvement of a catabolic organelle in growth signaling may have important implications for our understanding of mTORC1-related pathologies.

Indexed as

Amino AcidsDiabetes MellitusHumansLysosomesMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesNeoplasmsNeurodegenerative DiseasesTOR Serine-Threonine KinasesAmino AcidsMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesTOR Serine-Threonine Kinases

Identifiers

PMID22749019
PMCPMC3432651
OpenAlexW2059716825

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.