Architecture of the human mTORC2 core complex

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...

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Autores principales: Stuttfeld, Edward, Aylett, Christopher HS, Imseng, Stefan, Boehringer, Daniel, Scaiola, Alain, Sauer, Evelyn, Hall, Michael N, Maier, Timm, Ban, Nenad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2018
Materias:
Structural Biology and Molecular Biophysics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5837792/
https://www.ncbi.nlm.nih.gov/pubmed/29424687
http://dx.doi.org/10.7554/eLife.33101
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author Stuttfeld, Edward
Aylett, Christopher HS
Imseng, Stefan
Boehringer, Daniel
Scaiola, Alain
Sauer, Evelyn
Hall, Michael N
Maier, Timm
Ban, Nenad
author_facet Stuttfeld, Edward
Aylett, Christopher HS
Imseng, Stefan
Boehringer, Daniel
Scaiola, Alain
Sauer, Evelyn
Hall, Michael N
Maier, Timm
Ban, Nenad
author_sort Stuttfeld, Edward
collection PubMed
description 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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spelling pubmed-58377922018-03-07 Architecture of the human mTORC2 core complex Stuttfeld, Edward Aylett, Christopher HS Imseng, Stefan Boehringer, Daniel Scaiola, Alain Sauer, Evelyn Hall, Michael N Maier, Timm Ban, Nenad eLife Structural Biology and Molecular Biophysics 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. eLife Sciences Publications, Ltd 2018-02-09 /pmc/articles/PMC5837792/ /pubmed/29424687 http://dx.doi.org/10.7554/eLife.33101 Text en © 2018, Stuttfeld et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Structural Biology and Molecular Biophysics
Stuttfeld, Edward
Aylett, Christopher HS
Imseng, Stefan
Boehringer, Daniel
Scaiola, Alain
Sauer, Evelyn
Hall, Michael N
Maier, Timm
Ban, Nenad
Architecture of the human mTORC2 core complex
title Architecture of the human mTORC2 core complex
title_full Architecture of the human mTORC2 core complex
title_fullStr Architecture of the human mTORC2 core complex
title_full_unstemmed Architecture of the human mTORC2 core complex
title_short Architecture of the human mTORC2 core complex
title_sort architecture of the human mtorc2 core complex
topic Structural Biology and Molecular Biophysics
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5837792/
https://www.ncbi.nlm.nih.gov/pubmed/29424687
http://dx.doi.org/10.7554/eLife.33101
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