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

Target of rapamycin (TOR) kinase operates within two distinct multiprotein complexes named TORC1 and TORC2. Here the authors report a cryo-EM structure of TORC2, establish its subunit organization, providing a rationale for TORC2’s rapamycin insensitivity and the mutually exclusive inclusion of Avo3...

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Main Authors: Manikandan Karuppasamy, Beata Kusmider, Taiana M. Oliveira, Christl Gaubitz, Manoel Prouteau, Robbie Loewith, Christiane Schaffitzel
Format: Article
Language:English
Published: Nature Publishing Group 2017-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-01862-0
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spelling doaj-38eaa2c38bd64378bd64e3cfa22e39752021-05-11T07:38:48ZengNature Publishing GroupNature Communications2041-17232017-11-018111010.1038/s41467-017-01862-0Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2Manikandan Karuppasamy0Beata Kusmider1Taiana M. Oliveira2Christl Gaubitz3Manoel Prouteau4Robbie Loewith5Christiane Schaffitzel6European Molecular Biology Laboratory, Grenoble OutstationDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of GenevaEuropean Molecular Biology Laboratory, Grenoble OutstationDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of GenevaDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of GenevaDepartment of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of GenevaEuropean Molecular Biology Laboratory, Grenoble OutstationTarget of rapamycin (TOR) kinase operates within two distinct multiprotein complexes named TORC1 and TORC2. Here the authors report a cryo-EM structure of TORC2, establish its subunit organization, providing a rationale for TORC2’s rapamycin insensitivity and the mutually exclusive inclusion of Avo3/Rictor or Raptor within their respective TOR complex.https://doi.org/10.1038/s41467-017-01862-0
collection DOAJ
language English
format Article
sources DOAJ
author Manikandan Karuppasamy
Beata Kusmider
Taiana M. Oliveira
Christl Gaubitz
Manoel Prouteau
Robbie Loewith
Christiane Schaffitzel
spellingShingle Manikandan Karuppasamy
Beata Kusmider
Taiana M. Oliveira
Christl Gaubitz
Manoel Prouteau
Robbie Loewith
Christiane Schaffitzel
Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2
Nature Communications
author_facet Manikandan Karuppasamy
Beata Kusmider
Taiana M. Oliveira
Christl Gaubitz
Manoel Prouteau
Robbie Loewith
Christiane Schaffitzel
author_sort Manikandan Karuppasamy
title Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2
title_short Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2
title_full Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2
title_fullStr Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2
title_full_unstemmed Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2
title_sort cryo-em structure of saccharomyces cerevisiae target of rapamycin complex 2
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-11-01
description Target of rapamycin (TOR) kinase operates within two distinct multiprotein complexes named TORC1 and TORC2. Here the authors report a cryo-EM structure of TORC2, establish its subunit organization, providing a rationale for TORC2’s rapamycin insensitivity and the mutually exclusive inclusion of Avo3/Rictor or Raptor within their respective TOR complex.
url https://doi.org/10.1038/s41467-017-01862-0
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