Evidence map›Paper›PMID 27040916›Full record

ArticleNature communications2016

mTORC1 and CK2 coordinate ternary and eIF4F complex assembly.

Valentina Gandin, Laia Masvidal, Marie Cargnello, Laszlo Gyenis, Shannon McLaughlan, Yutian Cai, Clara Tenkerian, Masahiro Morita, Preetika Balanathan, Olivier Jean-Jean and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

64 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Regulation of cancer progression by CK2: an emerging therapeutic target.Medical oncology (Northwood, London, England) · 2024
    Review
  19. Article
  20. Review

4 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

19 authors at 10 institutions in 5 countries.

Valentina GandinLady Davis Institute, SMBD JGH, McGill University, Montreal, Quebec, Canada H3T 1E2.
Laia MasvidalDepartment of Oncology-Pathology, Science for Life Laboratory, Karolinska Institutet, Stockholm 171 76, Sweden.
Marie CargnelloLady Davis Institute, SMBD JGH, McGill University, Montreal, Quebec, Canada H3T 1E2.
Laszlo GyenisDepartments of Biochemistry and Oncology, Schulich School of Medicine &Dentistry, Western University, London, Ontario, Canada N6A 4L6.
Shannon McLaughlanLady Davis Institute, SMBD JGH, McGill University, Montreal, Quebec, Canada H3T 1E2.
Yutian CaiLady Davis Institute, SMBD JGH, McGill University, Montreal, Quebec, Canada H3T 1E2.
Clara TenkerianLady Davis Institute, SMBD JGH, McGill University, Montreal, Quebec, Canada H3T 1E2.
Masahiro MoritaDepartment of Biochemistry, McGill University, Montreal, Quebec, Canada H3T 1E2.
Preetika BalanathanCancer Program, Biomedicine Discovery Institute and Department of Anatomy and Developmental Biology, Monash University, Victoria 3168, Australia.
Olivier Jean-JeanUPMC Univ Paris 06, CNRS-UMR8256, Paris 75005, France.
Vuk StambolicPrincess Margaret Cancer Centre, University Health Network, and the Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Matthias TrostMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Scotland DD1 5EH, UK.ORCID http://orcid.org/0000-0002-5732-700X
Luc FuricCancer Program, Biomedicine Discovery Institute and Department of Anatomy and Developmental Biology, Monash University, Victoria 3168, Australia.
Louise LaroseDepartment of Medicine, Polypeptide Laboratory, McGill University and The Research Institute of McGill University Health Centre, Montreal, Quebec, Canada H3A 2B2.
Antonis E KoromilasLady Davis Institute, SMBD JGH, McGill University, Montreal, Quebec, Canada H3T 1E2.
Katsura AsanoMolecular Cellular and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, Kansas 66506, USA.
David LitchfieldDepartments of Biochemistry and Oncology, Schulich School of Medicine &Dentistry, Western University, London, Ontario, Canada N6A 4L6.
Ola LarssonDepartment of Oncology-Pathology, Science for Life Laboratory, Karolinska Institutet, Stockholm 171 76, Sweden.
Ivan TopisirovicLady Davis Institute, SMBD JGH, McGill University, Montreal, Quebec, Canada H3T 1E2.ORCID http://orcid.org/0000-0002-5510-9762
Jewish General Hospital · CAWestern University · CADiscovery Institute · USScience for Life Laboratory · SECentre National de la Recherche Scientifique · FRKansas State University · USMcGill University · CAMcGill University Health Centre · CAMRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Toronto · CA

Funding

CIHR MOP-115195CIHR MOP-37854CIHR MOP-38160Medical Research Council MC_UP_A500_1020Medical Research Council MC_UU_12016/5
6 · The paper itself

Abstract

Ternary complex (TC) and eIF4F complex assembly are the two major rate-limiting steps in translation initiation regulated by eIF2α phosphorylation and the mTOR/4E-BP pathway, respectively. How TC and eIF4F assembly are coordinated, however, remains largely unknown. We show that mTOR suppresses translation of mRNAs activated under short-term stress wherein TC recycling is attenuated by eIF2α phosphorylation. During acute nutrient or growth factor stimulation, mTORC1 induces eIF2β phosphorylation and recruitment of NCK1 to eIF2, decreases eIF2α phosphorylation and bolsters TC recycling. Accordingly, eIF2β mediates the effect of mTORC1 on protein synthesis and proliferation. In addition, we demonstrate a formerly undocumented role for CK2 in regulation of translation initiation, whereby CK2 stimulates phosphorylation of eIF2β and simultaneously bolsters eIF4F complex assembly via the mTORC1/4E-BP pathway. These findings imply a previously unrecognized mode of translation regulation, whereby mTORC1 and CK2 coordinate TC and eIF4F complex assembly to stimulate cell proliferation.

Indexed as

Adaptor Proteins, Signal TransducingCasein Kinase IIEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-4FGene Expression RegulationHEK293 CellsHumansMCF-7 CellsMechanistic Target of Rapamycin Complex 1Models, GeneticMultiprotein ComplexesOncogene ProteinsPeptide Chain Initiation, TranslationalPhosphorylationSignal TransductionStress, PhysiologicalAdaptor Proteins, Signal TransducingCasein Kinase IIEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-4FMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesNck proteinOncogene ProteinsTernary Complex FactorsTOR Serine-Threonine Kinases

Identifiers

PMID27040916
PMCPMC4822005
OpenAlexW2338181945

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.