Evidence map›Paper›PMID 23852728›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Feature Article: mTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology.

Charles Betz, Daniele Stracka, Cristina Prescianotto-Baschong, Maud Frieden, Nicolas Demaurex, Michael N Hall

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 299 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
299citing papers in PubMed, 2 pooled it
15.7field-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

299 citing papers in PubMed, 2 syntheses or guidelines pooled it, 519 citations in OpenAlex.

  1. Pooled it
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  8. The role of mTOR signaling in regulating the quality of mammalian oocytes.Journal of assisted reproduction and genetics · 2026
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  15. Mitochondria-ER crosstalk via MAMS: Bridging cellular homeostasis and cancer progression.Apoptosis : an international journal on programmed cell death · 2026
    Review
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239 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

6 authors at 2 institutions in 1 country.

Charles BetzGrowth and Development, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.
Daniele Stracka
Cristina Prescianotto-Baschong
Maud Frieden
Nicolas Demaurex
Michael N Hall
University of Basel · CHUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The target of rapamycin (TOR) is a highly conserved protein kinase and a central controller of growth. Mammalian TOR complex 2 (mTORC2) regulates AGC kinase family members and is implicated in various disorders, including cancer and diabetes. Here we report that mTORC2 is localized to the endoplasmic reticulum (ER) subcompartment termed mitochondria-associated ER membrane (MAM). mTORC2 localization to MAM was growth factor-stimulated, and mTORC2 at MAM interacted with the IP3 receptor (IP3R)-Grp75-voltage-dependent anion-selective channel 1 ER-mitochondrial tethering complex. mTORC2 deficiency disrupted MAM, causing mitochondrial defects including increases in mitochondrial membrane potential, ATP production, and calcium uptake. mTORC2 controlled MAM integrity and mitochondrial function via Akt mediated phosphorylation of the MAM associated proteins IP3R, Hexokinase 2, and phosphofurin acidic cluster sorting protein 2. Thus, mTORC2 is at the core of a MAM signaling hub that controls growth and metabolism.

Indexed as

AnimalsEndoplasmic ReticulumHeLa CellsHexokinaseHSP70 Heat-Shock ProteinsHumansInositol 1,4,5-Trisphosphate ReceptorsIntracellular MembranesMechanistic Target of Rapamycin Complex 2Membrane Potential, MitochondrialMembrane ProteinsMiceMice, KnockoutMitochondriaMultiprotein ComplexesProto-Oncogene Proteins c-aktglucose-regulated proteinsHexokinaseHSP70 Heat-Shock ProteinsInositol 1,4,5-Trisphosphate ReceptorsMechanistic Target of Rapamycin Complex 2Membrane ProteinsMultiprotein ComplexesProto-Oncogene Proteins c-aktTOR Serine-Threonine Kinases

Identifiers

PMID23852728
PMCPMC3732980
OpenAlexW2142583550

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.