Architecture of human Rag GTPase heterodimers and their complex with mTORC1

Anandapadamanaban M, Masson GR, Perisic O, Berndt A, Kaufman J, Johnson CM, Santhanam B, Rogala KB, Sabatini DM, Williams RL · 2019 · Science · Atlas ID ANA2019

What this study shows

Structures of Rag GTPase heterodimers with mTORC1 explain nucleotide-state-dependent recruitment.

Abstract

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The Rag guanosine triphosphatases (GTPases) recruit the master kinase mTORC1 to lysosomes to regulate cell growth and proliferation in response to amino acid availability. The nucleotide state of Rag heterodimers is critical for their association with mTORC1. Our cryo-electron microscopy structure of RagA/RagC in complex with mTORC1 shows the details of RagA/RagC binding to the RAPTOR subunit of mTORC1 and explains why only the RagA/RagCnucleotide state binds mTORC1. Previous kinetic studies suggested that GTP binding to one Rag locks the heterodimer to prevent GTP binding to the other.

Read the full abstract on PubMed →

At a glance

Evidence type	M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Cryo-EM structure) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is.
Study type	5 - Mechanistic / In Vitro
Model system	Cryo-EM structure
Journal	Science
Year	2019
Peer reviewed	Yes
Record last updated	2026-10-01
Source	DOI 10.1126/science.aax3939 · PMID 31601764 · Free full text (PMC6795536)

Extracted findings

These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.

Intervention	Structural (cryo-EM)
Target	RagA/RagC / RAPTOR / mTORC1
Model	Cryo-EM structure
Effect	Structure of RagA/RagC bound to mTORC1 (RAPTOR) explains nucleotide-state-dependent recruitment

In the Atlas

Links in the pathway map

Supports Rag GTPases recruits mTORC1

Cite this paper

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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. (2019). Architecture of human Rag GTPase heterodimers and their complex with mTORC1. Science. https://doi.org/10.1126/science.aax3939

@article{ANA2019,
  author       = {Anandapadamanaban, M. and Masson, G. R. and Perisic, O. and Berndt, A. and Kaufman, J. and Johnson, C. M. and Santhanam, B. and Rogala, K. B. and Sabatini, D. M. and Williams, R. L.},
  title        = {{Architecture of human Rag GTPase heterodimers and their complex with mTORC1}},
  journal      = {Science},
  year         = {2019},
  doi          = {10.1126/science.aax3939},
  note         = {PMID: 31601764},
}

Cite this Atlas record

The record is the Atlas's own work — the evidence label, the extracted findings and the links. It is cited as part of the dataset, not as the paper.

Barton, O. (2026). Oliver's mTOR Atlas (record ANA2019) [Data set]. https://mtor-atlas.org/study/ANA2019/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_ANA2019,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record ANA2019},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/ANA2019/},
  doi          = {10.5281/zenodo.22059963}
}

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