Growth factor signaling to mTORC1 by amino acid–laden macropinosomes
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The rapid activation of the mechanistic target of rapamycin complex-1 (mTORC1) by growth factors is increased by extracellular amino acids through yet-undefined mechanisms of amino acid transfer into endolysosomes. Because the endocytic process of macropinocytosis concentrates extracellular solutes into endolysosomes and is increased in cells stimulated by growth factors or tumor-promoting phorbol esters, we analyzed its role in amino acid–dependent activation of mTORC1. Here, we show that growth factor-dependent activation of mTORC1 by amino acids, but not glucose, requires macropinocytosis. In murine bone marrow–derived macrophages and murine embryonic fibroblasts stimulated with their cognate growth factors or with phorbol myristate acetate, activation of mTORC1 required an Akt-independent vesicular pathway of amino acid delivery into endolysosomes, mediated by the actin cytoskeleton. Macropinocytosis delivered small, fluorescent fluid-phase solutes into endolysosomes sufficiently fast to explain growth factor–mediated signaling by amino acids. Therefore, the amino acid–laden macropinosome is an essential and discrete unit of growth factor receptor signaling to mTORC1.
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TSC1/2 plays a major role in integrating insulin and growth factor signaling through the PI3K and AKT pathway, although recent data suggest growth factors may also stimulate mTORC1 by enhancing delivery of amino acid-laden macropinosomes to the Ragulator complex.
“This complex plays a major role in integrating insulin and growth factor signaling through the PI3K and AKT pathway (Figure 10), although recent data suggest growth factors may also stimulate mTORC1 by enhancing the delivery of amino acid-laden macropinosomes to the Ragulator complex (593).”
From Placental Origins of Chronic Disease (2016) · cites this paper as [593]
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Self-citationExploiting cancer’s drinking problem: regulation and therapeutic potential of macropinocytosis
Puccini, J., Badgley, M. A., & Bar‐Sagi, D. (2021) · Trends in cancer · doi:10.1016/j.trecan.2021.09.004 · Cited by 67 · see citing works
The physiological regulation of macropinocytosis during Dictyostelium growth and development
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Using macropinocytosis for intracellular delivery of therapeutic nucleic acids to tumour cells
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Proton-gated anion transport governs macropinosome shrinkage
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Loss of PTEN promotes formation of signaling-capable clathrin-coated pits
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Macropinosomes as units of signal transduction
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Self-citationIron Drives Anabolic Metabolism Through Active Histone Demethylation and mTORC1
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CXCL12-induced macropinocytosis modulates two distinct pathways to activate mTORC1 in macrophages
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Self-citationMacropinocytosis and Cancer: From Tumor Stress to Signaling Pathways
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Macropinocytosis and autophagy crosstalk in nutrient scavenging
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Intracellular Transport in Cancer Metabolic Reprogramming
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Dorsal ruffles enhance activation of Akt by growth factors
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Self-citationTargeted drug delivery system inspired by macropinocytosis
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PI3Kβ is selectively required for growth factor-stimulated macropinocytosis
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Rab8a localisation and activation by Toll-like receptors on macrophage macropinosomes
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Dynamin inhibitors block activation of mTORC1 by amino acids independently of dynamin
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Uptake of collagen type I via macropinocytosis cause mTOR activation and anti-cancer drug resistance
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Nox2-Mediated PI3K and Cofilin Activation Confers Alternate Redox Control of Macrophage Pinocytosis
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Acidic Ca2+ stores and immune-cell function
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Macropinocytosis Fuels Prostate Cancer
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Generation of somatic mitochondrial DNA-replaced cells for mitochondrial dysfunction treatment
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Signaling Pathways that Regulate Macropinocytosis in Mammalian Cells
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ATM inhibition drives metabolic adaptation via induction of macropinocytosis
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Clathrin-mediated endocytosis regulates fMLP-mediated neutrophil polarization
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Roles for 3’ Phosphoinositides in Macropinocytosis
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SLIT2/ROBO1 signaling suppresses mTORC1 for organelle control and bacterial killing
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Amino acids suppress macropinocytosis and promote release of CSF1 receptor in macrophages
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Self-citationLoss of PTEN promotes formation of signaling-capable clathrin-coated pitsPreprint
Rosselli-Murai, L. K., Yates, J. A., Yoshida, S., Bourg, J., Ho, K. K. Y., White, M., Prisby, J., Tan, X., Altemus, M., Bao, L., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/137760 · Cited by 7 · see citing works
Self-citationThe PtdIns3P-binding protein Phafin2 escorts macropinosomes through the cortical actin cytoskeletonPreprint
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Macropinosomes are a site of HIV-1 entry into primary CD4 + T cells
Murakami, T., Cardoso, R. D. S., Manivannan, P., Chang, Y.-T., Rentchler, E. C., Chou, K.-N., Tang, Y., Swanson, J. A., King, P. D., & Ono, A. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2417676122 · Cited by 5 · see citing works
Self-citationArf5-mediated regulation of mTORC1 at the plasma membrane
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WNK1 mediates M-CSF-induced macropinocytosis to enforce macrophage lineage fidelity
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Functional Diversity of Macropinocytosis
Mishra, R., Gupta, Y., Ghaley, G., & Bhowmick, N. A. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-94004-1_1 · Cited by 4 · see citing works
The role of leucine in the activation of cellular metabolism: a large integrative review
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Live Fluorescence, Inverse Imaging of Cell Ruffling, and Macropinocytosis
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ATP triggers macropinocytosis that internalizes and is regulated by PANX1Preprint
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Does mTORC1 inhibit autophagy at dual stages?
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Leucyl-tRNA synthetase 1 is required for proliferation of TSC-null cells
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Self-citationSize of lipid emulsion droplets influences metabolism in human CD4+ T cells
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Investigating the role of amino acid transporter LAT3/SLC43A1 in prostate cancer
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Self-citation
- Authors
- Yoshida, S., Pacitto, R., Yao, Y., Inoki, K., & Swanson, J. A.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Swanson, Joel A.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2015-10-05
- Volume
- 211
- Issue
- 1
- Pages
- 159-172
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC4602043
- OpenAlex
- W2179272349
- Cited by
- 105
- References
- 66
- Citations by year
- 2026: 3 · 2025: 11 · 2024: 6 · 2023: 9 · 2022: 15 · 2021: 11 · 2020: 9 · 2019: 4 · 2018: 16 · 2017: 13 · 2016: 8
- FWCI
- 5.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk083491-09)
- National Institute of General Medical Sciences (R01GM110215, R01-GM-110215-01)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK083491, R01DK124709)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mTORC1 activation, macropinocytosis, amino acid signaling, growth factor signaling, endolysosomes, phorbol myristate acetate, actin cytoskeleton, Akt-independent signaling, macrophages, embryonic fibroblasts, fluid-phase endocytosis
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Biological Transport, Fibroblasts, Humans, Macrophages, Mice, Inbred C57BL, Pinocytosis, Platelet-Derived Growth Factor, Endosomes, Signal Transduction, Macrophage Colony-Stimulating Factor, Multiprotein Complexes, HEK293 Cells, TOR Serine-Threonine Kinases
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