Thomas U. Schwartz
MIT structural biologist who studies how molecules pass across the nuclear envelope, and whose crystallography lab helped solve the leucine and arginine sensor structures upstream of mTORC1
Boris Magasanik Professor in Biology, Department of Biology, Massachusetts Institute of Technology · PhD, Free University of Berlin (2000)
Portrait: MIT Department of Biology
Thomas Schwartz is a co-author of two Atlas papers, made with David Sabatini's lab, on how mTORC1 senses amino acids. mTORC1, the growth-control complex, switches on only when amino acids are present, and sensor proteins report on single amino acids. SAX2015 gives the crystal structure of Sestrin2 holding leucine and shows a pocket closed by a lid-like loop. SAX2016 gives the structure of CASTOR1 holding arginine and shows how arginine binding makes CASTOR1 release GATOR2, lifting a brake on mTORC1. These are structures of purified proteins, backed by tests in cells. They turned the idea of an amino acid sensor into a picture at the level of atoms.
Schwartz's own research is on communication across biological membranes. The lab uses structural, biochemical and genetic tools to study how signals and molecules move between the nucleus and the cytoplasm through the nuclear envelope, and how the nuclear pore and its transport machinery are built. Schwartz earned a PhD at the Free University of Berlin in 2000 and is now the Boris Magasanik Professor in Biology at MIT.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2015 | M | Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway SAX2015 Co-author: the Schwartz crystallography lab helped solve the structure of Sestrin2 bound to leucine. |
| 2016 | M | Mechanism of arginine sensing by CASTOR1 upstream of mTORC1 SAX2016 Co-author: the Schwartz crystallography lab helped solve the structure of CASTOR1 bound to arginine. |
Co-authors in the Atlas 7
People with a profile here who share at least one study with Thomas U. Schwartz.
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- David M. Sabatini 2 shared studies Identified mTOR (as RAFT1) in 1994. His lab then mapped much of the machinery around it: raptor and rictor at the core of mTORC1 and mTORC2, the Rag–Ragulator system that docks mTORC1 on the lysosome, and the sensors that detect leucine, arginine and SAM
- Kevin E. Knockenhauer 2 shared studies Structural biologist trained in Thomas Schwartz's MIT lab who helped solve the amino acid sensor structures of Sestrin2 and CASTOR1, and who later moved to drug discovery at Accent Therapeutics
- Lynne Chantranupong 2 shared studies Showed as a Sabatini-lab graduate student that the Sestrins act through GATOR2 to regulate amino-acid signalling to mTORC1. She then discovered the CASTOR proteins, the cell's arginine sensors for the pathway
- Robert A. Saxton 2 shared studies Solved, as a Sabatini-lab graduate student, the structures of the leucine sensor Sestrin2 and the arginine sensor CASTOR1, showing how each one grips its amino acid. He also co-wrote a widely cited 2017 review of mTOR signalling with David Sabatini
- Michael E. Pacold Radiation oncologist and chemical biologist at NYU Langone who studies the metabolism of brain tumours, and a co-author of the Sabatini lab's structure of the leucine sensor Sestrin2
- Rachel L. Wolfson Identified Sestrin2 as the direct leucine sensor of the mTORC1 pathway as a Sabatini-lab MD-PhD student. She also co-discovered KICSTOR, the complex that recruits GATOR1 to the lysosome
- Tim Wang Co-developed genome-wide CRISPR screening in human cells (reported in parallel by Feng Zhang's lab) as a graduate student with David Sabatini and Eric Lander, and contributed to studies showing that the 4E-BPs mediate mTORC1's control of translation and that CASTOR1 senses arginine
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