Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway
Open accessAbstract
From sensing leucine to metabolic control: The mTORC1 protein kinase complex plays central roles in regulating cell growth and metabolism and is implicated in common human diseases such as diabetes and cancer. The level of the amino acid leucine tells an organism a lot about its physiological state, including how much food is available, how much insulin is going to be needed, and whether new muscle mass can be made (see the Perspective by Buel and Blenis). Wolfson et al. identified a biochemical sensor of leucine, Sestrin2, which connects the concentration of leucine to the control of organismal metabolism and growth. When leucine bound to Sestrin2, it was released from a complex with the mTORC1 regulatory factor GATOR2, activating the mTORC1 complex. Saxton et al. describe the crystal structure of Sestrin2 and show how it specifically detects leucine. Aylett et al. determined the structure of human mTORC1 by cryoelectron microscopy and the crystal structure of a regulatory subunit, Raptor. The results reveal the structural basis for the function and intricate regulation of this important enzyme, which is also a strategic drug target. Science , this issue p. 43 , p. 48 , p. 53 ; see also p. 25
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mTORC1 is activated by leucine via sestrin 1/2.
“and by leucine, which binds to the leucine sensors sestrin 1/2 [174, 175]”
From Effects of Skeletal Muscle Hypertrophy on Fat Mass and Glucose Homeostasis in Humans and Animals: A Narrative Review with Systematic Literature Search (2025) · cites this paper as [175]
The Abstract and Conclusions establish that leucine binds Sestrin2 and that this sensing regulates mTORC1 activation. The paper does not establish that leucine binds Sestrin1; the cell experiment mentions Sestrin1 only as one of three Sestrins knocked out before Sestrin2 was reintroduced. (LLM, conf=0.88)
Experimental — accuracy not yet measuredLeucine activates mTORC1 signaling by binding to the upstream regulator sestrin.
“notably including the amino acid leucine, which activates mTORC1 signaling via binding to the upstream regulator sestrin.”
From Sestrin modulator NV-5138 produces rapid antidepressant effects via direct mTORC1 activation (2019) · cites this paper as [21]
Leucine binds to sestrin isoforms 1 and 2, causing dissociation from GATOR2 and activation of mTORC1 signaling.
“Recent studies demonstrate that leucine binds to sestrin isoforms 1 and 2 (hereafter referred to as sestrin), resulting in dissociation from another regulatory multiprotein complex, GATOR2, leading to activation of mTORC1 signaling (20, 21).”
From Sestrin modulator NV-5138 produces rapid antidepressant effects via direct mTORC1 activation (2019) · cites this paper as [21]
Mutations of Sestrin2 that block leucine binding also block leucine activation of mTORC1 signaling.
“Further evidence for this pathway is provided by studies demonstrating that mutations of Sestrin2 that block leucine binding also block leucine activation of mTORC1 signaling (20, 21).”
From Sestrin modulator NV-5138 produces rapid antidepressant effects via direct mTORC1 activation (2019) · cites this paper as [21]
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- Authors
- Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., & Sabatini, D. M.
- Affiliations
- Broad Institute (US)
- Massachusetts Institute of Technology (US)
- Corresponding author
- Sabatini, David M.
- ORCID
- Venue
- Science
- Published
- 2016-01
- Volume
- 351
- Issue
- 6268
- Pages
- 53-58
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4698039
- OpenAlex
- W2231368253
- Cited by
- 457
- References
- 46
- Citations by year
- 2026: 34 · 2025: 39 · 2024: 36 · 2023: 47 · 2022: 42 · 2021: 52 · 2020: 57 · 2019: 37 · 2018: 43 · 2017: 33 · 2016: 36 · 2015: 1
- FWCI
- 16.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- National Institute of General Medical Sciences
- National Institutes of Health (P41 GM103403)
- NIH-ORIP HEI (S10 RR029205)
- Argonne National Laboratory (DE-AC02-06CH11357)
- U.S. Department of Defense (W81XWH-07-0448)
- NIH (T32GM007287, R01CA103866, AI47389, T32 GM007753, F30 CA189333, F31 CA180271, F31 CA189437)
- MIT Whitaker Health Sciences Fund
- Damon Runyon Cancer Research Foundation (DRG-112-12)
- Department of Defense Breast Cancer Research (BC120208)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- Sestrin2, mTORC1, leucine sensing, amino acid sensing, GATOR2, raptors, kinase regulation, crystal structure, cryo-EM structure, cell growth regulation, metabolic control, therapeutic target
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Sestrins, Amino Acid Sequence, Binding Sites, Humans, Leucine, Molecular Sequence Data, Mutation, Nuclear Proteins, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Multiprotein Complexes, Metabolic Networks and Pathways, HEK293 Cells, TOR Serine-Threonine Kinases
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