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Architecture of human Rag GTPase heterodimers and their complex with mTORC1

Anandapadamanaban, Madhanagopal, Masson, Glenn R., Perisic, Olga, Berndt, Alex, Kaufman, Jonathan, Johnson, Chris M., Santhanam, Balaji, Rogala, Kacper B., Sabatini, David M., Williams, Roger L.·2019·Science
DOI 10.1126/science.aax3939PMC PMC6795536
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Abstract

Mastering regulation: The mechanistic target of rapamycin complex 1 (mTORC1) is known as the master kinase, acknowledging its key role in integrating multiple signals to regulate cell growth. When nutrients are abundant, heterodimers of Rag, a class of small guanosine triphosphatase, bind to mTORC1 and recruit it to the lysosome. Here, other signaling pathways converge on the mTORC1 complex. Anandapadamanaban et al. determined cryo–electron microscopy and crystal structures of a RagA/RagC heterodimer. The structures, together with dynamic studies, explain the nucleotide states required for binding to mTORC1 and support a mechanism for conformational communication between the RagA and RagC subunits in the heterodimer. RagA/RagC binding causes no conformational change in mTORC1, which is consistent with the idea that mTORC1 must sense additional growth regulators before it is activated. Science , this issue p. 203

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Metadata

Authors
Anandapadamanaban, M., Masson, G. R., Perisic, O., Berndt, A., Kaufman, J., Johnson, C. M., Santhanam, B., Rogala, K. B., Sabatini, D. M., & Williams, R. L.
Affiliations
  • MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
  • Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2019-10-11
Volume
366
Issue
6462
Pages
203-210
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.aax3939
PMC
PMC6795536
Cited by
147
References
15
Language
en
Funders
  • National Institutes of Health (R01 CA103866, R01 CA129105, R37 AI047389)
  • U.S. Department of Defense (W81XWH15-1-0230)
  • Howard Hughes Medical Institute
  • American Cancer Society
  • Saint Catharine's College
  • Medical Research Council (MC_U105184308)
  • Cancer Research UK (C14801/A21211)
  • Lustgarten Foundation
  • European Molecular Biology Organization (ALTF 1171-2016)
  • Federation of European Biochemical Societies
  • Tuberous Sclerosis Association
  • Company of Biologists
  • Royal Society of Chemistry

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