ArticleProceedings of the National Academy of Sciences of the United States of America2014
Stoichiometry and assembly of mTOR complexes revealed by single-molecule pulldown.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 62 citations in OpenAlex.
- Targeting the GSK-3β/mTOR axis: a novel pharmacological strategy for preeclampsia prevention and treatment.Naunyn-Schmiedeberg's archives of pharmacology · 2026Review
- The Fantastic Single-Molecule Techniques.Chemical & biomedical imaging · 2026Review
- Protocol for Nanodisc single-molecule pull-down assay to detect protein-lipid interactions.STAR protocols · 2026Article
- SiMPull-POP: Quantification of Membrane Protein Assembly via Single Molecule Photobleaching.Bio-protocol · 2026Article
- Exploring Biophysics at the Membrane with Single-Molecule TIRF Microscopy.Advances in experimental medicine and biology · 2026Review
- Bayesian analysis and efficient algorithms for single-molecule fluorescence data and step counting.Biophysical journal · 2025Article
- Single-Molecule Protein Interactions and Unfolding Revealed by Plasmon-Enhanced Fluorescence.Analytical chemistry · 2025Article
- Bayesian analysis and efficient algorithms for single-molecule fluorescence data and step counting.bioRxiv : the preprint server for biology · 2025Article
- A universal chimeric antigen receptor (CAR)-fragment antibody binder (FAB) split system for cancer immunotherapy.Science advances · 2025Article
- Conformation-specific synthetic intrabodies modulate mTOR signaling with subcellular spatial resolution.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multifocal, multiphenotypic tumours arising from an MTOR mutation acquired in early embryogenesis.Oncogene · 2024Article
- Direct observation of autoubiquitination for an integral membrane ubiquitin ligase in ERAD.Nature communications · 2024Article
- Mind your tag in single-molecule measurements.Cell reports methods · 2023Article
- The START domain potentiates HD-ZIPIII transcriptional activity.The Plant cell · 2023Article
- Article
- Bi-allelic TTI1 variants cause an autosomal-recessive neurodevelopmental disorder with microcephaly.American journal of human genetics · 2023Article
- Label-Free Single-Molecule Pulldown for the Detection of Released Cellular Protein Complexes.ACS central science · 2022Article
- AAA + ATPase Thorase inhibits mTOR signaling through the disassembly of the mTOR complex 1.Nature communications · 2022Article
- A DAP5/eIF3d alternate mRNA translation mechanism promotes differentiation and immune suppression by human regulatory T cells.Nature communications · 2021Article
- SARS-CoV-2 Neuronal Invasion and Complications: Potential Mechanisms and Therapeutic Approaches.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The mammalian target of rapamycin (mTOR) kinase is a master regulator of cellular, developmental, and metabolic processes. Deregulation of mTOR signaling is implicated in numerous human diseases including cancer and diabetes. mTOR functions as part of either of the two multisubunit complexes, mTORC1 and mTORC2, but molecular details about the assembly and oligomerization of mTORCs are currently lacking. We use the single-molecule pulldown (SiMPull) assay that combines principles of conventional pulldown assays with single-molecule fluorescence microscopy to investigate the stoichiometry and assembly of mTORCs. After validating our approach with mTORC1, confirming a dimeric assembly as previously reported, we show that all major components of mTORC2 exist in two copies per complex, indicating that mTORC2 assembles as a homodimer. Interestingly, each mTORC component, when free from the complexes, is present as a monomer and no single subunit serves as the dimerizing component. Instead, our data suggest that dimerization of mTORCs is the result of multiple subunits forming a composite surface. SiMPull also allowed us to distinguish complex disassembly from stoichiometry changes. Physiological conditions that abrogate mTOR signaling such as nutrient deprivation or energy stress did not alter the stoichiometry of mTORCs. On the other hand, rapamycin treatment leads to transient appearance of monomeric mTORC1 before complete disruption of the mTOR-raptor interaction, whereas mTORC2 stoichiometry is unaffected. These insights into assembly of mTORCs may guide future mechanistic studies and exploration of therapeutic potential.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.