Evidence map›Paper›PMID 27072897›Full record

ArticleNature communications2016

Tor forms a dimer through an N-terminal helical solenoid with a complex topology.

Domagoj Baretić, Alex Berndt, Yohei Ohashi, Christopher M Johnson, Roger L Williams

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 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
7.8field-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

51 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
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  18. Article
  19. Review
  20. Transcriptional Regulation of NK Cell Development by mTOR Complexes.Frontiers in cell and developmental biology · 2020
    Review
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 at 1 institution in 1 country.

Domagoj BaretićMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Alex BerndtMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.ORCID http://orcid.org/0000-0001-6822-6098
Yohei OhashiMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Christopher M JohnsonMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Roger L WilliamsMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184308Medical Research Council U105184308
6 · The paper itself

Abstract

The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 heterodimer forms a common sub-complex. We have determined the cryo-electron microscopy (EM) structure of Tor bound to Lst8. Two Tor-Lst8 heterodimers assemble further into a dyad-symmetry dimer mediated by Tor-Tor interactions. The first 1,300 residues of Tor form a HEAT repeat-containing α-solenoid with four distinct segments: a highly curved 800-residue N-terminal 'spiral', followed by a 400-residue low-curvature 'bridge' and an extended 'railing' running along the bridge leading to the 'cap' that links to FAT region. This complex topology was verified by domain insertions and offers a new interpretation of the mTORC1 structure. The spiral of one TOR interacts with the bridge of another, which together form a joint platform for the Regulatory Associated Protein of TOR (RAPTOR) regulatory subunit.

Indexed as

Protein MultimerizationAnimalsCatalytic DomainCryoelectron MicroscopyHumansKluyveromycesMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2MiceModels, MolecularMultiprotein ComplexesProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Multiprotein ComplexesSaccharomyces cerevisiae ProteinsTOR Serine-Threonine Kinases

Identifiers

PMID27072897
PMCPMC4833857
OpenAlexW2336647682

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.