Evidence map›Paper›PMID 28143890›Full record

ArticleThe Journal of cell biology2017

Localization of mTORC2 activity inside cells.

Michael Ebner, Benjamin Sinkovics, Magdalena Szczygieł, Daniela Wolfschoon Ribeiro, Ivan Yudushkin

Abstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

136 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. mTORC2-NaChannels (Austin, Tex.) · 2026
    Article
  3. Review
  4. Infection and immunity · 2026
    Article
  5. Article
  6. Article
  7. bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. The insulin signalling network.Nature metabolism · 2025
    Review
  14. mTOR Signaling in Macrophages: All Depends on the Context.International journal of molecular sciences · 2025
    Review
  15. Article
  16. Review
  17. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  18. Article
  19. Article
  20. Review

76 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

5 authors.

Michael EbnerMax F. Perutz Laboratories, Department of Structural and Computational Biology, Vienna BioCenter, 1030 Vienna, Austria.ORCID http://orcid.org/0000-0003-4234-7187
Benjamin SinkovicsDepartment of Medical Biochemistry, Medical University of Vienna, 1030 Vienna, Austria.
Magdalena SzczygiełVienna BioCenter Summer School Program, Division of Systems Biology of Signal Transduction, 69120 Heidelberg, Germany.
Daniela Wolfschoon RibeiroCenter for Molecular Biology, Student Services, University of Vienna, 1030 Vienna, Austria.
Ivan YudushkinMax F. Perutz Laboratories, Department of Structural and Computational Biology, Vienna BioCenter, 1030 Vienna, Austria ivan.yudushkin@mfpl.ac.at.ORCID http://orcid.org/0000-0002-6637-027X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of protein kinase Akt via its direct phosphorylation by mammalian target of rapamycin (mTOR) complex 2 (mTORC2) couples extracellular growth and survival cues with pathways controlling cell growth and proliferation, yet how growth factors target the activity of mTORC2 toward Akt is unknown. In this study, we examine the localization of the obligate mTORC2 component, mSin1, inside cells and report the development of a reporter to examine intracellular localization and regulation by growth factors of the endogenous mTORC2 activity. Using a combination of imaging and biochemical approaches, we demonstrate that inside cells, mTORC2 activity localizes to the plasma membrane, mitochondria, and a subpopulation of endosomal vesicles. We show that unlike the endosomal pool, the activity and localization of mTORC2 via the Sin1 pleckstrin homology domain at the plasma membrane is PI3K and growth factor independent. Furthermore, we show that membrane recruitment is sufficient for Akt phosphorylation in response to growth factors. Our results indicate the existence of spatially separated mTORC2 populations with distinct sensitivity to PI3K inside cells and suggest that intracellular localization could contribute to regulation of mTORC2 activity toward Akt.

Indexed as

Carrier ProteinsCell MembraneEndosomesHEK293 CellsHeLa CellsHumansMCF-7 CellsMechanistic Target of Rapamycin Complex 2Microscopy, ConfocalMitochondriaMonomeric GTP-Binding ProteinsMultiprotein ComplexesPhosphorylationProtein Interaction Domains and MotifsProto-Oncogene Proteins c-aktRecombinant Fusion ProteinsCarrier ProteinsMechanistic Target of Rapamycin Complex 2Monomeric GTP-Binding ProteinsmSin1 protein, humanMultiprotein ComplexesProto-Oncogene Proteins c-aktRecombinant Fusion ProteinsTOR Serine-Threonine Kinases

Identifiers

PMID28143890
PMCPMC5294791

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.