Architecture of the human mTORC2 core complex

Edward Stuttfeld; Christopher Hs Aylett; Stefan Imseng; Daniel Boehringer; Alain Scaiola; Evelyn Sauer; Michael N Hall; Timm Maier; Nenad Ban

doi:10.7554/eLife.33101

Architecture of the human mTORC2 core complex

Elife. 2018 Feb 9:7:e33101. doi: 10.7554/eLife.33101.

Authors

Affiliations

¹ Biozentrum, University of Basel, Basel, Switzerland.
² Institute for Molecular Biology and Biophysics, Zürich, Switzerland.

^# Contributed equally.

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.

Keywords: cell growth; electron microscopy; human; molecular biophysics; regulation; structural biology.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cryoelectron Microscopy*
Humans
Mechanistic Target of Rapamycin Complex 2 / chemistry*
Mechanistic Target of Rapamycin Complex 2 / metabolism*
Models, Molecular
Protein Binding
Protein Conformation

Substances

Mechanistic Target of Rapamycin Complex 2

Abstract

Publication types

MeSH terms

Substances

Grants and funding