Evidence map›Paper›PMID 28264193›Full record

ArticleeLife2017

Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit.

Hisashi Tatebe, Shinichi Murayama, Toshiya Yonekura, Tomoyuki Hatano, David Richter, Tomomi Furuya, Saori Kataoka, Kyoko Furuita, Chojiro Kojima, Kazuhiro Shiozaki

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

46 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Article
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  4. RICTOR variants are associated with neurodevelopmental disorders.European journal of human genetics : EJHG · 2025
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  6. Clear cell renal carcinoma essentially requires CDKL3 for oncogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. mTORC2: a multifaceted regulator of autophagy.Cell communication and signaling : CCS · 2023
    Review
  15. Article
  16. Protein kinase C: release from quarantine by mTORC2.Trends in biochemical sciences · 2022
    Review
  17. Structural insights into Ras regulation by SIN1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. New mechanistic insights into the RAS-SIN1 interaction at the membrane.Frontiers in cell and developmental biology · 2022
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Hisashi TatebeGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
Shinichi MurayamaGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
Toshiya YonekuraGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
Tomoyuki HatanoGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
David RichterDepartment of Microbiology and Molecular Genetics, University of California, California, United States.
Tomomi FuruyaGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
Saori KataokaInstitute for Protein Research, Osaka University, Osaka, Japan.
Kyoko FuruitaInstitute for Protein Research, Osaka University, Osaka, Japan.
Chojiro KojimaInstitute for Protein Research, Osaka University, Osaka, Japan.
Kazuhiro ShiozakiGraduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.ORCID 0000-0002-0395-5457
Nara Institute of Science and Technology · JPProtein Research Foundation · JPUniversity of California, Los Angeles · USYokohama National University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The target of rapamycin (TOR) protein kinase forms multi-subunit TOR complex 1 (TORC1) and TOR complex 2 (TORC2), which exhibit distinct substrate specificities. Sin1 is one of the TORC2-specific subunit essential for phosphorylation and activation of certain AGC-family kinases. Here, we show that Sin1 is dispensable for the catalytic activity of TORC2, but its conserved region in the middle (Sin1CRIM) forms a discrete domain that specifically binds the TORC2 substrate kinases. Sin1CRIM fused to a different TORC2 subunit can recruit the TORC2 substrate Gad8 for phosphorylation even in the

Indexed as

Adaptor Proteins, Signal TransducingCarrier ProteinsConserved SequenceHEK293 CellsHumansMagnetic Resonance SpectroscopyMechanistic Target of Rapamycin Complex 2Models, MolecularProtein BindingProtein ConformationProtein FoldingProtein Interaction MappingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSubstrate SpecificityAdaptor Proteins, Signal TransducingCarrier ProteinsMAPKAP1 protein, humanMechanistic Target of Rapamycin Complex 2Schizosaccharomyces pombe ProteinsSin1 protein, S pombeAKTbiochemistrycell biologyhumanSIN1S. pombesubstrate specificitytarget of rapamycinTOR complex 2

Identifiers

PMID28264193
PMCPMC5340527
OpenAlexW2591793663

What OpenQuestion holds

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Registered trials

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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.