Evidence map›Paper›PMID 21909137›Full record

ArticleOncogene2012

Integrity of mTORC2 is dependent on the rictor Gly-934 site.

R Aimbetov, C-H Chen, O Bulgakova, D Abetov, A K Bissenbaev, R I Bersimbaev, D D Sarbassov

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Regulatory effects of mTORC2 complexes in type I IFN signaling and in the generation of IFN responses.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
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

7 authors at 4 institutions in 2 countries.

R AimbetovDepartment of Molecular and Cellular Oncology, University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
C-H Chen
O Bulgakova
D Abetov
A K Bissenbaev
R I Bersimbaev
D D Sarbassov
Al-Farabi Kazakh National University · KZL. N. Gumilyov Eurasian National University · KZThe University of Texas MD Anderson Cancer Center · USUniversity of Houston · US

Funding

The mTORC2 signaling in breast cancerR01CA133522 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI SARBASSOV, DOS DJURMAKHANBET · 2009 to 2013
$1.6M
NCI NIH HHS CA133522NCI NIH HHS R01 CA133522
6 · The paper itself

Abstract

Growth factor signaling coupled to activation of the phosphatidylinositol-3-OH kinase (PI3K)/Akt pathway plays a crucial role in the regulation of cell proliferation and survival. The key regulatory kinase of Akt has been identified as mammalian target of rapamycin complex 2 (mTORC2), which functions as the PI3K-dependent Ser-473 kinase of Akt. This kinase complex is assembled by mTOR and its essential components rictor, Sin1 and mLST8. The recent genetic screening study in Caenorhabditis elegans has linked a specific point mutation of rictor to an elevated storage of fatty acids that resembles the rictor deficiency phenotype. In our study, we show that in mammalian cells the analogous single rictor point mutation (G934E) prevents the binding of rictor to Sin1 and the assembly of mTORC2, but this mutation does not interfere with the binding of the rictor-interacting protein Protor. A substitution of the rictor Gly-934 residue to a charged amino acid prevents formation of the rictor/Sin1 heterodimer. The cells expressing the rictor G934E mutant remain deficient in the mTORC2 signaling, as detected by the reduced phosphorylation of Akt on Ser-473 and a low cell proliferation rate. Thus, although a full length of rictor is required to interact with its binding partner Sin1, a single amino acid of rictor Gly-934 controls its interaction with Sin1 and assembly of mTORC2.

Indexed as

Adaptor Proteins, Signal TransducingCarrier ProteinsGlycineHumansPoint MutationRapamycin-Insensitive Companion of mTOR ProteinTranscription FactorsAdaptor Proteins, Signal TransducingCarrier ProteinsCRTC2 protein, humanGlycineMAPKAP1 protein, humanRapamycin-Insensitive Companion of mTOR ProteinRICTOR protein, humanTranscription Factors

Identifiers

PMID21909137
PMCPMC3305845
OpenAlexW2073368001

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.