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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2017-11-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-01862-0 |
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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 |
work_keys_str_mv |
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1721451741167222784 |