Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2

Karuppasamy M, Kusmider B, Oliveira TM, Gaubitz C, Prouteau M, Loewith R, Schaffitzel C · 2017 · Nature communications · Atlas ID KAR2017

What this study shows

Cryo-EM structure of yeast TORC2 reveals its overall architecture and rapamycin insensitivity.

Abstract

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The target of rapamycin (TOR) kinase assembles into two distinct multiprotein complexes, conserved across eukaryote evolution. In contrast to TOR complex 1 (TORC1), TORC2 kinase activity is not inhibited by the macrolide rapamycin. Here, we present the structure of Saccharomyces cerevisiae TORC2 determined by electron cryo-microscopy. TORC2 contains six subunits assembling into a 1.4 MDa rhombohedron. Tor2 and Lst8 form the common core of both TOR complexes.

Read the full abstract on PubMed →

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	2017
Peer reviewed	Yes
Record last updated	2026-10-01
Source	DOI 10.1038/s41467-017-01862-0 · PMID 29170376 · Free full text (PMC5700991)

Extracted findings

These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.

Intervention	Structural (cryo-EM)
Target	TORC2 (Tor2/Lst8/Avo)
Model	Cryo-EM structure (S. cerevisiae)
Effect	Cryo-EM structure of yeast TORC2, a 1.4-MDa rhombohedron of six subunits

In the Atlas

Links in the pathway map

Supports mTOR required-for mTORC2

Cite this paper

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Karuppasamy, M., Kusmider, B., Oliveira, T. M., Gaubitz, C., Prouteau, M., Loewith, R., & Schaffitzel, C. (2017). Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2. Nature communications. https://doi.org/10.1038/s41467-017-01862-0

@article{KAR2017,
  author       = {Karuppasamy, M. and Kusmider, B. and Oliveira, T. M. and Gaubitz, C. and Prouteau, M. and Loewith, R. and Schaffitzel, C.},
  title        = {{Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2}},
  journal      = {Nature communications},
  year         = {2017},
  doi          = {10.1038/s41467-017-01862-0},
  note         = {PMID: 29170376},
}

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 KAR2017) [Data set]. https://mtor-atlas.org/study/KAR2017/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_KAR2017,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record KAR2017},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/KAR2017/},
  doi          = {10.5281/zenodo.22059963}
}

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