Author
Listed:
- Manuele Rebsamen
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Lorena Pochini
(Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy)
- Taras Stasyk
(Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)
- Mariana E. G. de Araújo
(Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)
- Michele Galluccio
(Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy)
- Richard K. Kandasamy
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Berend Snijder
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Astrid Fauster
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Elena L. Rudashevskaya
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Present address: Institute of Medical Chemistry, Medical University of Vienna, 1090 Vienna, Austria.)
- Manuela Bruckner
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Stefania Scorzoni
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Przemyslaw A. Filipek
(Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)
- Kilian V. M. Huber
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Johannes W. Bigenzahn
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Leonhard X. Heinz
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Claudine Kraft
(Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria)
- Keiryn L. Bennett
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
- Cesare Indiveri
(Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy)
- Lukas A. Huber
(Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria)
- Giulio Superti-Furga
(CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria)
Abstract
The mTORC1 protein kinase complex integrates nutrient and growth stimuli to modulate signalling pathways that regulate cellular metabolism and physiology, but the molecular nature of the amino acid sensing mechanism at the lysosome is unknown; here, an orphan member of the human solute carrier group of proteins, SLC38A9, is shown to be an integral component of the lysosomal machinery that can directly sense amino acids and activate mTORC1.
Suggested Citation
Manuele Rebsamen & Lorena Pochini & Taras Stasyk & Mariana E. G. de Araújo & Michele Galluccio & Richard K. Kandasamy & Berend Snijder & Astrid Fauster & Elena L. Rudashevskaya & Manuela Bruckner & St, 2015.
"SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1,"
Nature, Nature, vol. 519(7544), pages 477-481, March.
Handle:
RePEc:nat:nature:v:519:y:2015:i:7544:d:10.1038_nature14107
DOI: 10.1038/nature14107
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Citations
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Cited by:
- Lior Artzi & Assaf Alon & Kelly P. Brock & Anna G. Green & Amy Tam & Fernando H. Ramírez-Guadiana & Debora Marks & Andrew Kruse & David Z. Rudner, 2021.
"Dormant spores sense amino acids through the B subunits of their germination receptors,"
Nature Communications, Nature, vol. 12(1), pages 1-8, December.
- Zhenzhen Zi & Zhuzhen Zhang & Qiang Feng & Chiho Kim & Xu-Dong Wang & Philipp E. Scherer & Jinming Gao & Beth Levine & Yonghao Yu, 2022.
"Quantitative phosphoproteomic analyses identify STK11IP as a lysosome-specific substrate of mTORC1 that regulates lysosomal acidification,"
Nature Communications, Nature, vol. 13(1), pages 1-12, December.
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