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

Manikandan Karuppasamy; Beata Kusmider; Taiana M. Oliveira; Christl Gaubitz; Manoel Prouteau; Robbie Loewith; Christiane Schaffitzel

doi:10.1038/s41467-017-01862-0

Nature Communications (Nov 2017)

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

Manikandan Karuppasamy,
Beata Kusmider,
Taiana M. Oliveira,
Christl Gaubitz,
Manoel Prouteau,
Robbie Loewith,
Christiane Schaffitzel

Affiliations

Manikandan Karuppasamy: European Molecular Biology Laboratory, Grenoble Outstation
Beata Kusmider: Department of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva
Taiana M. Oliveira: European Molecular Biology Laboratory, Grenoble Outstation
Christl Gaubitz: Department of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva
Manoel Prouteau: Department of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva
Robbie Loewith: Department of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva
Christiane Schaffitzel: European Molecular Biology Laboratory, Grenoble Outstation

DOI: https://doi.org/10.1038/s41467-017-01862-0
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 10

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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