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.
CeMM, Vienna · Scientific Director (since 2005) · Professor of Medical Systems Biology, Medical University of Vienna (since 2015)
Portrait: Superti-Furga Lab, CeMM
Giulio Superti-Furga is the scientific director of CeMM, the Research Center for Molecular Medicine of the Austrian Academy of Sciences in Vienna, and a professor of medical systems biology at the Medical University of Vienna. Earlier he led a team at EMBL in Heidelberg and co-founded the company Cellzome.
His group uses large-scale proteomics to see which proteins sit together in cells and how drugs act on them. A big interest is the solute carrier (SLC) family, proteins that carry nutrients and other small molecules across membranes.
In the 2015 Nature paper in the Atlas (first author Manuele Rebsamen, with Lukas Huber's group in Innsbruck and others), the team described SLC38A9 as a protein in the lysosome membrane that can transport amino acids. It binds the Ragulator and Rag GTPase machinery, and cells without it responded poorly to amino acids. SLC38A9 thus became one of the lysosomal sensors that tell mTORC1 when amino acids are available.
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 Identified SLC38A9 as a lysosomal amino-acid transporter and part of the Ragulator-Rag machinery required for amino-acid activation of mTORC1; Superti-Furga was senior author. |
Co-authors in the Atlas 3
People with a profile here who share at least one study with Giulio Superti-Furga.
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- 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
- 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
- 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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