Manuele Rebsamen
Cell biologist who found that the lysosomal transporter SLC38A9 is part of the amino acid sensor for mTORC1, and who now leads a group at the University of Lausanne studying transporters in immune signalling and autoimmunity
Group leader, Department of Immunobiology, University of Lausanne (from about 2022) · CeMM Research Center for Molecular Medicine, Vienna, Giulio Superti-Furga lab (about 2013–2022) · University of Lausanne, Juerg Tschopp lab (2008–2012)
mTORC1, the growth-control complex, is switched on at the surface of the lysosome when amino acids are plentiful. In 2015, as first author of a Nature paper from Giulio Superti-Furga's group at CeMM in Vienna, Manuele Rebsamen showed that SLC38A9, an amino acid transporter in the lysosome membrane, binds the Ragulator-Rag machinery that brings mTORC1 there. Cells with extra SLC38A9 kept mTORC1 active even when amino acids were removed, and cells without it switched mTORC1 on poorly when amino acids returned. These are cell studies.
Rebsamen began in innate immunity. In Juerg Tschopp's lab at the University of Lausanne, Rebsamen co-authored work on how cells detect RNA viruses, including the role of TRADD in the RIG-I antiviral pathway (2008) and inflammasome activation by RIG-I (2009). At CeMM, Rebsamen focused on solute carriers, the large family of membrane transporters, including a 2020 classification of human transporters by what they carry and a 2022 genetic screen for transporters that help cells survive nutrient shortage. Rebsamen was also a co-author of the 2018 Science paper identifying LZTR1 as a regulator of RAS.
Rebsamen now leads a group at the Department of Immunobiology of the University of Lausanne in Epalinges. The lab studies how the lysosomal transporter SLC15A4 and its partner TASL control immune signals from Toll-like receptors, and in 2025 and 2026 showed that this complex is needed for antiviral responses and for lupus-like autoimmune disease in mice.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2015 | M | SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1 REB2015 First author: identified SLC38A9 as a lysosomal amino acid transporter that is part of the Ragulator-Rag sensing machinery for mTORC1. |
Co-authors in the Atlas 3
People with a profile here who share at least one study with Manuele Rebsamen.
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- Giulio Superti-Furga Systems biologist who maps how proteins and drugs interact in cells, with a focus on solute carrier (SLC) membrane transporters; his group helped identify SLC38A9 as a lysosomal amino-acid sensor for mTORC1.
- Lukas A. Huber Cell biologist who studied the p14-MP1 scaffold on late endosomes, a complex later recognised as part of Ragulator (LAMTOR), the lysosomal platform that holds mTORC1 in place
- Taras Stasyk Protein chemist in Lukas Huber's group in Innsbruck who has spent two decades applying proteomics to the late endosomes and lysosomes where mTORC1 is controlled
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