Architecture of the human mTORC2 core complex

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Cite this article as: eLife 2018;7:e33101 doi: 10.7554/eLife.33101

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Abstract

The mammalian target of rapamycin (mTOR) is a key protein kinase controlling cellular metabolism and growth. It is part of the two structurally and functionally distinct multiprotein complexes mTORC1 and mTORC2. Dysregulation of mTOR occurs in diabetes, cancer and neurological disease. We report the architecture of human mTORC2 at intermediate resolution, revealing a conserved binding site for accessory proteins on mTOR and explaining the structural basis for the rapamycin insensitivity of the complex.

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Edward Stuttfeld

Biozentrum, University of Basel, Basel, Switzerland

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0003-3932-9076
Christopher H S Aylett

Institute for Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland

Competing interests
The authors declare that no competing interests exist.
Stefan Imseng

Biozentrum, University of Basel, Basel, Switzerland

Competing interests
The authors declare that no competing interests exist.
Daniel Boehringer

Institute for Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland

Competing interests
The authors declare that no competing interests exist.
Alain Scaiola

Institute for Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland

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The authors declare that no competing interests exist.
Evelyn Sauer

Biozentrum, University of Basel, Basel, Switzerland

Competing interests
The authors declare that no competing interests exist.
Michael N Hall

Biozentrum, University of Basel, Basel, Switzerland

For correspondence
m.hall@unibas.ch

Competing interests
The authors declare that no competing interests exist.
Timm Maier

Biozentrum, University of Basel, Basel, Switzerland

For correspondence
timm.maier@unibas.ch

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0002-7459-1363
Nenad Ban

Institute for Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland

For correspondence
ban@mol.biol.ethz.ch

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0002-9527-210X

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (51NF40_141735_NCCR)

Nenad Ban

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (310030_159492)

Michael N Hall

European Research Council (609883)

Michael N Hall

Sir Henry Dale Fellowship (206212/Z/17/Z)

Christopher H S Aylett

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (138262)

Nenad Ban

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (159696)

Timm Maier

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (310030B_163478)

Nenad Ban

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Reviewing Editor

Nahum Sonenberg, McGill University, Canada

Publication history

Received: October 25, 2017
Accepted: February 8, 2018
Accepted Manuscript published: February 9, 2018 (version 1)
Version of Record published: March 5, 2018 (version 2)

Copyright

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.