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Structural basis for the docking of mTORC1 on the lysosomal surface
Abstract
Complex regulation: The protein kinase mTORC1 controls cellular growth in response to external signals. In the presence of nutrients, it localizes on the surface of the lysosome, where it is activated. The Raptor domain of mTORC1 binds to a complex comprising the protein Ragulator and a heterodimer of the Rag guanosine triphosphatase, which can adopt four different nucleotide conformations depending on nutrient availability. Rogala et al. determined the structure of the Raptor-Rag-Ragulator complex at 3.2-angstrom resolution by cryo–electron microscopy. The structure shows why Raptor binds only to a specific nucleotide conformation of the Rag heterodimer and suggests a model for how mTORC1 would dock onto the lysosomal surface, which is a key step in its activation. Science , this issue p. 468
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“High-resolution structures have also been generated of the complexes that regulate mTORC1 activity, including the TSC complex 158, the Rag GTPases in complex with mTORC1 and Ragulator 159–161, and the binding of leucine by Sestrin2 162.”
From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [161]
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Metadata
- Authors
- Rogala, K. B., Gu, X., Kedir, J. F., Abu-Remaileh, M., Bianchi, L. F., Bottino, A. M. S., Dueholm, R., Niehaus, A., Overwijn, D., Fils, A.-C. P., Zhou, S. X., Leary, D., Laqtom, N. N., Brignole, E. J., & Sabatini, D. M.
- Affiliations
- Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
- Broad Institute of Harvard and MIT, Cambridge, MA 02142, USA.
- Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
- ORCID
- Venue
- Science
- Published
- 2019-10-25
- Volume
- 366
- Issue
- 6464
- Pages
- 468-475
- ISSN
- 0036-8075
- 1095-9203
- PMC
- PMC7176403
- Cited by
- 214
- References
- 15
- Language
- en
- Funders
- National Institutes of Health (R01 CA103866, R01 CA129105, R37 AI47389, F30 CA236179)
- U.S. Department of Defense (W81XWH-07-0448)
- Howard Hughes Medical Institute
- Charles A. King Trust
- Koch Institute
- American Cancer Society
- Lustgarten Foundation
- Saudi Aramco Ibn Khaldun Fellowship for Saudi Women
- Tuberous Sclerosis Association
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- The paper
- Rogala, K. B., Gu, X., Kedir, J. F., Abu-Remaileh, M., Bianchi, L. F., Bottino, A. M. S., Dueholm, R., Niehaus, A., Overwijn, D., Fils, A.-C. P., Zhou, S. X., Leary, D., Laqtom, N. N., Brignole, E. J., & Sabatini, D. M. (2019). Structural basis for the docking of mTORC1 on the lysosomal surface. Science. https://doi.org/10.1126/science.aay0166