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

Baretic D, Williams RL et al. · 2016 · Nature communications · Atlas ID BAR2016

What this study shows

Cryo-EM shows TOR dimerizes through an N-terminal helical solenoid, informing mTORC1 architecture.

Abstract

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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.

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At a glance

Evidence type	M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Cryo-EM structure) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is.
Study type	5 - Mechanistic / In Vitro
Model system	Cryo-EM structure
Journal	Nature communications
Year	2016
Peer reviewed	Yes
Record last updated	2026-08-22
Source	DOI 10.1038/ncomms11016 · PMID 27072897 · Free full text (PMC4833857)

Extracted findings

Intervention	Structural (cryo-EM)
Target	TOR / Lst8
Model	Cryo-EM structure
Effect	Tor-Lst8 heterodimers assemble into a dyad-symmetric dimer via Tor-Tor interactions (N-terminal solenoid)

Cite this paper

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Baretic, D., et al. (2016). Tor forms a dimer through an N-terminal helical solenoid with a complex topology. Nature communications. https://doi.org/10.1038/ncomms11016

@article{BAR2016,
  author       = {Baretic, D. and Williams, R. L. and others},
  title        = {{Tor forms a dimer through an N-terminal helical solenoid with a complex topology}},
  journal      = {Nature communications},
  year         = {2016},
  doi          = {10.1038/ncomms11016},
  note         = {PMID: 27072897},
}

Cite this Atlas record

The record is the Atlas's own work — the evidence label, the extracted findings and the links. It is cited as part of the dataset, not as the paper.

Barton, O. (2026). Oliver's mTOR Atlas (record BAR2016) [Data set]. https://mtor-atlas.org/study/BAR2016/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_BAR2016,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record BAR2016},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/BAR2016/},
  doi          = {10.5281/zenodo.22059963}
}